Continued with EC 4.2.1.101 to EC 4.2.1.183
EC 4.2.1.101 to EC 4.2.1.183
Accepted name: prephenate dehydratase
Reaction: prephenate = phenylpyruvate + H2O + CO2
For diagram click here.
Other name(s): prephenate hydro-lyase (decarboxylating)
Systematic name: prephenate hydro-lyase (decarboxylating; phenylpyruvate-forming)
Comments: This enzyme in the enteric bacteria also possesses chorismate mutase (EC 5.4.99.5) activity, and converts chorismate into prephenate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9044-88-6
References:
1. Cerutti, P. and Guroff, G. Enzymatic formation of phenylpyruvic acid in Pseudomonas sp. (ATCC 11299A) and its regulation. J. Biol. Chem. 240 (1965) 3034-3048. [PMID: 14342329]
2. Cotton, R.G.H. and Gibson, F. The biosynthesis of phenylalanine and tyrosine; enzymes converting chorismic acid into prephenic acid and their relationships to prephenate dehydratase and prephenate dehydrogenase. Biochim. Biophys. Acta 100 (1965) 76-88.
3. Schmidt, J.C. and Zalkin, H. Chorismate mutase-prephenate dehydratase. Partial purification and properties of the enzyme from Salmonella typhimurium. Biochemistry 8 (1969) 174-181.
[EC 4.2.1.52 Transferred entry: dihydrodipicolinate synthase. Now EC 4.3.3.7, 4-hydroxy-2,3,4,5-tetrahydrodipicolinate synthase. (EC 4.2.1.52 created 1972, transferred 2012 to EC 4.3.3.7, deleted 2012)]
Accepted name: oleate hydratase
Reaction: (R)-10-hydroxystearate = oleate + H2O
Other name(s): (R)-10-hydroxystearate 10-hydro-lyase
Systematic name: (R)-10-hydroxystearate 10-hydro-lyase (oleate-forming)
Comments: Acts on a number of 10-hydroxy acids.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9073-51-2
References:
1. Davis, E.N., Wallen, L.L., Goodwin, J.C., Rohwedder, W.K. and Rhodes, R.A. Microbial hydration of cis-9-alkenoic acids. Lipids 4 (1969) 356-362. [PMID: 5823715]
2. Gotouda, H., Takatori, T., Terazawa, K., Nagao, M. and Tarao, H. The mechanism of experimental adipocere formation: hydration and dehydrogenation in microbial synthesis of hydroxy and oxo fatty acids. Forensic Sci. Int. 37 (1988) 249-257. [PMID: 3410394]
3. Niehaus, W.G., Jr., Kisic, A., Torkelson, A., Bednarczyk, D.J. and Schroepfer, G.J., Jr., Stereospecific hydration of the δ9 double bond of oleic acid. J. Biol. Chem. 245 (1970) 3790-3797. [PMID: 5492948]
Accepted name: lactoyl-CoA dehydratase
Reaction: (R)-lactoyl-CoA = acryloyl-CoA + H2O
Other name(s): lactoyl coenzyme A dehydratase; lactyl-coenzyme A dehydrase; lactyl CoA dehydratase; acrylyl coenzyme A hydratase; lactoyl-CoA hydro-lyase
Systematic name: (R)-lactoyl-CoA hydro-lyase (acryloyl-CoA-forming)
Comments: A bacterial enzyme that is involved in propanoate fermentation (also known as the acrylate pathway).
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, CAS registry number: 9031-12-3
References:
1. Baldwin, R.L., Wood, W.A. and Emery, R.S. Lactate metabolism by Peptostreptococcus elsdenii: evidence for lactyl coenzyme a dehydrase. Biochim. Biophys. Acta 97 (1965) 202-213. [PMID: 14292829]
2. Schweiger, G. and Buckel, W. On the dehydration of (R)-lactate in the fermentation of alanine to propionate by Clostridium propionicum. FEBS Lett 171 (1984) 79-84. [PMID: 6586495]
3. Kuchta, R.D. and Abeles, R.H. Lactate reduction in Clostridium propionicum. Purification and properties of lactyl-CoA dehydratase. J. Biol. Chem. 260 (1985) 13181-13189. [PMID: 4055736]
4. Kuchta, R.D., Hanson, G.R., Holmquist, B. and Abeles, R.H. Fe-S centers in lactyl-CoA dehydratase. Biochemistry 25 (1986) 7301-7307. [PMID: 3026450]
5. Hofmeister, A.E. and Buckel, W. (R)-Lactyl-CoA dehydratase from Clostridium propionicum. Stereochemistry of the dehydration of (R)-2-hydroxybutyryl-CoA to crotonyl-CoA. Eur. J. Biochem. 206 (1992) 547-552. [PMID: 1597194]
Accepted name: 3-hydroxybutyryl-CoA dehydratase
Reaction: (3R)-3-hydroxybutanoyl-CoA = crotonoyl-CoA + H2O
For diagram of reaction click here.
Other name(s): D-3-hydroxybutyryl coenzyme A dehydratase; D-3-hydroxybutyryl-CoA dehydratase; enoyl coenzyme A hydrase (D); (3R)-3-hydroxybutanoyl-CoA hydro-lyase
Systematic name: (3R)-3-hydroxybutanoyl-CoA hydro-lyase (crotonoyl-CoA-forming)
Comments: Also acts on crotonoyl thioesters of pantetheine and acyl-carrier protein.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37290-82-7
References:
1. Moskowitz, G.J. and Merrick, J.M. Metabolism of poly-β-hydroxybutyrate. II. Enzymatic synthesis of D-(–)-β hydroxybutyryl coenzyme A by an enoyl hydrase from Rhodospirillum rubrum. Biochemistry 8 (1969) 2748-2755. [PMID: 5808333]
Accepted name: itaconyl-CoA hydratase
Reaction: citramalyl-CoA = itaconyl-CoA + H2O
Other name(s): itaconyl coenzyme A hydratase; citramalyl-CoA hydro-lyase
Systematic name: citramalyl-CoA hydro-lyase (itaconyl-CoA-forming)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37290-83-8
References:
1. Cooper, R.A. and Kornberg, H.L. The utilization of itaconate by Pseudomonas sp. Biochem. J. 91 (1964) 82-91. [PMID: 4284209]
Accepted name: isohexenylglutaconyl-CoA hydratase
Reaction: 3-hydroxy-3-(4-methylpent-3-en-1-yl)glutaryl-CoA = 3-(4-methylpent-3-en-1-yl)pent-2-enedioyl-CoA + H2O
Other name(s): 3-hydroxy-3-isohexenylglutaryl-CoA-hydrolase; isohexenylglutaconyl coenzyme A hydratase; β-isohexenylglutaconyl-CoA-hydratase; 3-hydroxy-3-(4-methylpent-3-en-1-yl)glutaryl-CoA hydro-lyase
Systematic name: 3-hydroxy-3-(4-methylpent-3-en-1-yl)glutaryl-CoA hydro-lyase [3-(4-methylpent-3-en-1-yl)pent-2-enedioyl-CoA-forming]
Comments: Also acts on dimethylacryloyl-CoA and farnesoyl-CoA.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, CAS registry number: 37290-84-9
References:
1. Seubert, W. and Fass, E. Untersuchungen über den bakterielle Abbau von Isoprenoiden. IV. Reinigung und Eigenschaftender β-Isohexenylglutaconyl-CoA-hydratase und β-Hydroxy-β-isohexenylglutaryl-CoA-lyase. Biochem. Z. 341 (1964) 23-34.
[EC 4.2.1.58 Deleted entry: crotonoyl-[acyl-carrier-protein] hydratase. The reaction described is covered by EC 4.2.1.59. (EC 4.2.1.58 created 1972, deleted 2012)]
Accepted name: 3-hydroxyacyl-[acyl-carrier-protein] dehydratase
Reaction: a (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl-carrier protein] + H2O
Other name(s): fabZ (gene name); fabA (gene name); D-3-hydroxyoctanoyl-[acyl carrier protein] dehydratase; D-3-hydroxyoctanoyl-acyl carrier protein dehydratase; β-hydroxyoctanoyl-acyl carrier protein dehydrase; β-hydroxyoctanoyl thioester dehydratase; β-hydroxyoctanoyl-ACP-dehydrase; (3R)-3-hydroxyoctanoyl-[acyl-carrier-protein] hydro-lyase; (3R)-3-hydroxyoctanoyl-[acyl-carrier-protein] hydro-lyase (oct-2-enoyl-[acyl-carrier protein]-forming); 3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase
Systematic name: (3R)-3-hydroxyacyl-[acyl-carrier protein] hydro-lyase (trans-2-enoyl-[acyl-carrier protein]-forming)
Comments: This enzyme is responsible for the dehydration step of the dissociated (type II) fatty-acid biosynthesis system that occurs in plants and bacteria. The enzyme uses fatty acyl thioesters of ACP in vivo. Different forms of the enzyme may have preferences for substrates with different chain length. For example, the activity of FabZ, the ubiquitous enzyme in bacteria, decreases with increasing chain length. Gram-negative bacteria that produce unsaturated fatty acids, such as Escherichia coli, have another form (FabA) that prefers intermediate chain length, and also catalyses EC 5.3.3.14, trans-2-decenoyl-[acyl-carrier protein] isomerase. Despite the differences both forms can catalyse all steps leading to the synthesis of palmitate (C16:0). FabZ, but not FabA, can also accept unsaturated substrates [4].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9030-85-7
References:
1. Mizugaki, M., Swindell, A.C. and Wkil, S.J. Intermediate- and long-chain β-hydroxyacyl-ACP dehydrases from E. coli fatty acid synthetase. Biochem. Biophys. Res. Commun. 33 (1968) 520-527. [PMID: 4881058]
2. Sharma, A., Henderson, B.S., Schwab, J.M. and Smith, J.L. Crystallization and preliminary X-ray analysis of β-hydroxydecanoyl thiol ester dehydrase from Escherichia coli. J. Biol. Chem. 265 (1990) 5110-5112. [PMID: 2180957]
3. Mohan, S., Kelly, T.M., Eveland, S.S., Raetz, C.R. and Anderson, M.S. An Escherichia coli gene (FabZ) encoding (3R)-hydroxymyristoyl acyl carrier protein dehydrase. Relation to fabA and suppression of mutations in lipid A biosynthesis. J. Biol. Chem. 269 (1994) 32896-32903. [PMID: 7806516]
4. Heath, R.J. and Rock, C.O. Roles of the FabA and FabZ β-hydroxyacyl-acyl carrier protein dehydratases in Escherichia coli fatty acid biosynthesis. J. Biol. Chem. 271 (1996) 27795-27801. [PMID: 8910376]
[EC 4.2.1.60 Deleted entry: 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase. The reaction described is covered by EC 4.2.1.59. (EC 4.2.1.60 created 1972, modified 2006, deleted 2012)]
[EC 4.2.1.61 Deleted entry: 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase. The reaction described is covered by EC 4.2.1.59. (EC 4.2.1.61 created 1972, deleted 2012)]
Accepted name: 5α-hydroxysteroid dehydratase
Reaction: 5α-ergosta-7,22-diene-3β,5-diol = ergosterol + H2O
Other name(s): 5α-ergosta-7,22-diene-3β,5-diol 5,6-hydro-lyase
Systematic name: 5α-ergosta-7,22-diene-3β,5-diol 5,6-hydro-lyase (ergosterol-forming)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9075-27-8
References:
1. Topham, R.W. and Gaylor, J.L. Isolation and purification of a 5α-hydroxysterol dehydrase of yeast. J. Biol. Chem. 245 (1970) 2319-2327. [PMID: 5442273]
[EC 4.2.1.63 Transferred entry: now EC 3.3.2.3 epoxide hydrolase (EC 4.2.1.63 created 1972, deleted 1978)]
[EC 4.2.1.64 Transferred entry: now EC 3.3.2.3 epoxide hydrolase (EC 4.2.1.64 created 1972, deleted 1978)]
Accepted name: 3-cyanoalanine hydratase
Reaction: L-asparagine = 3-cyanoalanine + H2O
Other name(s): β-cyanoalanine hydrolase; β-cyanoalanine hydratase; β-CNAla hydrolase; β-CNA nitrilase; L-asparagine hydro-lyase
Systematic name: L-asparagine hydro-lyase (3-cyanoalanine-forming)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37259-64-6
References:
1. Castric, P.A., Farnden, K.J.F. and Conn, E.E. Cyanide metabolism in higher plants. V. The formation of asparagine from β-cyanoalanine. Arch. Biochem. Biophys. 152 (1972) 62-69. [PMID: 4627358]
Accepted name: cyanide hydratase
Reaction: formamide = cyanide + H2O
Other name(s): formamide dehydratase; formamide hydro-lyase
Systematic name: formamide hydro-lyase (cyanide-forming)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37292-83-4
References:
1. Fry, W.E. and Millar, R.L. Cyanide degradion by an enzyme from Stemphylium loti. Arch. Biochem. Biophys. 151 (1972) 468-474. [PMID: 5065258]
Accepted name: D-fuconate dehydratase
Reaction: D-fuconate = 2-dehydro-3-deoxy-D-fuconate + H2O
Other name(s): D-fuconate hydro-lyase
Systematic name: D-fuconate hydro-lyase (2-dehydro-3-deoxy-D-fuconate-forming)
Comments: Also acts on L-arabinonate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9076-59-9
References:
1. Dahms, A.S. and Anderson, R.L. D-Fucose metabolism in a pseudomonad. 3. Conversion of D-fuconate to 2-keto-3-deoxy-D-fuconate by a dehydratase. J. Biol. Chem. 247 (1972) 2233-2237. [PMID: 4335868]
Accepted name: L-fuconate dehydratase
Reaction: L-fuconate = 2-dehydro-3-deoxy-L-fuconate + H2O
For diagram of reaction click here
Other name(s): L-fuconate hydro-lyase
Systematic name: L-fuconate hydro-lyase (2-dehydro-3-deoxy-L-fuconate-forming)
Comments: Also acts, slowly, on D-arabinonate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37292-84-5
References:
1. Yuen, R. and Schachter, H. L-Fucose metabolism in mammals. I. Pork liver L-fuconate hydro-lyase. Can. J. Biochem. 50 (1972) 798-806. [PMID: 5050937]
Accepted name: cyanamide hydratase
Reaction: urea = cyanamide + H2O
Other name(s): urea hydro-lyase
Systematic name: urea hydro-lyase (cyanamide-forming)
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 50812-20-9
References:
1. Stransky, H. and Amberger, A. Isolation and properties of a cyanamide hydratase (EC 4.2.1) from Myrothecium verrucaria. Z. Pflanzenphysiol. 70 (1973) 74-87.
Accepted name: pseudouridylate synthase
Reaction: uracil + D-ribose 5-phosphate = pseudouridine 5'-phosphate + H2O
Other name(s): pseudouridylic acid synthetase; pseudouridine monophosphate synthetase; 5-ribosyluracil 5-phosphate synthetase; pseudouridylate synthetase; upsilonUMP synthetase; uracil hydro-lyase (adding D-ribose 5-phosphate); YeiN; pseudouridine-5'-phosphate glycosidase
Systematic name: uracil hydro-lyase (adding D-ribose 5-phosphate; pseudouridine-5'-phosphate-forming)
Comments: The reaction it readily reversible. While the enzymes from Tetrahymena pyriformis and Agrobacterium tumefaciens produce pseudouridine 5'-phosphate the enzyme from Escherichia coli functions as a pseudouridine-5'-phosphate glycosidase in vivo [5].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9023-35-2
References:
1. Heinrikson, R.L. and Goldwasser, E. Studies on the biosynthesis of 5-ribosyluracil 5'-monophosphate in Tetrahymena pyriformis. J. Biol. Chem. 239 (1964) 1177-1187. [PMID: 14165924]
2. Matsushita, T. and Davis, F.F. Studies on pseudouridylic acid synthetase from various sources. Biochim. Biophys. Acta 238 (1971) 165-173. [PMID: 4936431]
3. Rensen, J.F., Matsushita, T., Chirikjian, J.G. and Davis, F.F. Enzymatic synthesis of deoxypseudouridylic acid and a study of certain of its properties. Biochim. Biophys. Acta 281 (1972) 481-487. [PMID: 4569284]
4. Suzuki, T. and Hochater, R.M. On the biosynthesis of pseudouridine and of pseudouridylic acid in Agrobacterium tumefaciens. Can. J. Biochem. 44 (1966) 259-272. [PMID: 5942965]
5. Preumont, A., Snoussi, K., Stroobant, V., Collet, J.F. and Van Schaftingen, E. Molecular identification of pseudouridine-metabolizing enzymes. J. Biol. Chem. 283 (2008) 25238-25246. [PMID: 18591240]
[EC 4.2.1.71 Deleted entry: acetylenecarboxylate hydratase. This enzyme is identical to EC 4.2.1.27, acetylenecarboxylate hydratase (EC 4.2.1.71 created 1978, modified 1989, modified 2000, deleted 2004)]
[EC 4.2.1.72 Transferred entry: acetylenedicarboxylate hydratase. Now EC 4.1.1.78, acetylenedicarboxylate decarboxylase (EC 4.2.1.72 created 1978, deleted 2000)]
Accepted name: protoaphin-aglucone dehydratase (cyclizing)
Reaction: protoaphin aglucone = xanthoaphin + H2O
Other name(s): protoaphin dehydratase; protoaphin dehydratase (cyclizing); protoaphin-aglucone hydro-lyase (cyclizing)
Systematic name: protoaphin-aglucone hydro-lyase (cyclizing; xanthoaphin-forming)
Comments: The product is converted non-enzymically to erythroaphin, an aphid pigment.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 64177-87-3
References:
1. Cameron, D.W., Sawyer, W.H. and Trikojus, V.M. Colouring matters of the Aphidoidea. XLII. Purification and properties of the cyclising enzyme [Protoaphin dehydratase (cyclising)] concerned with pigment transformation in the wooly aphid Eriosoma lanigerum Hausmann (Hemiptera: Insecta). Aust. J. Biol. Sci. 30 (1977) 173-181.
Accepted name: medium-chain-enoyl-CoA hydratase
Reaction: a medium-chain (3S)-3-hydroxyacyl-CoA = a medium-chain trans-2-enoyl-CoA + H2O
Glossary: a medium-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains 6 to 12 carbon atoms.
Other name(s): long-chain enoyl coenzyme A hydratase (incorrect); long-chain-enoyl-CoA hydratase (incorrect); long-chain-(3S)-3-hydroxyacyl-CoA hydro-lyase (incorrect)
Systematic name: medium-chain-(3S)-3-hydroxyacyl-CoA hydro-lyase
Comments: Acts in the reverse direction. The best substrate for the porcine enzyme is oct-2-enoyl-CoA. Unlike EC 4.2.1.17 enoyl-CoA hydratase, it does not act on crotonoyl-CoA.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 62009-81-8
References:
1. Fong, J.C. and Schulz, H. Purification and properties of pig heart crotonase and the presence of short chain and long chain enoyl coenzyme A hydratases in pig and guinea pig tissues. J. Biol. Chem. 252 (1977) 542-547. [PMID: 833142]
2. Schulz, H. Long chain enoyl coenzyme A hydratase from pig heart. J. Biol. Chem. 249 (1974) 2704-2709. [PMID: 4828315]
3. Arent, S., Christensen, C.E., Pye, V.E., Norgaard, A. and Henriksen, A. The multifunctional protein in peroxisomal β-oxidation: structure and substrate specificity of the Arabidopsis thaliana protein MFP2. J. Biol. Chem. 285 (2010) 24066-24077. [PMID: 20463021]
Accepted name: uroporphyrinogen-III synthase
Reaction: hydroxymethylbilane = uroporphyrinogen III + H2O
For diagram of reaction click here (mechanism).
Other name(s): porphobilinogenase; uroporphyrinogen isomerase; uroporphyrinogen III cosynthase; URO-synthase; hydroxymethylbilane hydro-lyase (cyclizing)
Systematic name: hydroxymethylbilane hydro-lyase (cyclizing; uroporphyrinogen-III-forming)
Comments: In the presence of EC 2.5.1.61, hydroxymethylbilane synthase, the enzyme forms uroporphyrinogen III from porphobilinogen.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37340-55-9
References:
1. Battersby, A.R., Fookes, C.J.R., Matcham, G.W.J. and McDonald, E. Biosynthesis of the pigments of life: formation of the macrocycle. Nature 285 (1980) 17-21. [PMID: 6769048]
2. Tsai, S.-F., Bishop, D.F. and Desnick, R.J. Purification and properties of uroporphyrinogen III synthase from human erythrocytes. J. Biol. Chem. 262 (1987) 1268-1273. [PMID: 3805019]
Accepted name: UDP-glucose 4,6-dehydratase
Reaction: UDP-α-D-glucose = UDP-4-dehydro-6-deoxy-α-D-glucose + H2O
For diagram of reaction click here.
Other name(s): UDP-D-glucose-4,6-hydrolyase; UDP-D-glucose oxidoreductase; UDP-glucose 4,6-hydro-lyase
Systematic name: UDP-α-D-glucose 4,6-hydro-lyase (UDP-4-dehydro-6-deoxy-α-D-glucose-forming)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 68189-53-7
References:
1. Kamsteeg, J., van Brederode, J. and van Nigtevecht, G. The formation of UDP-L-rhamnose from UDP-D-glucose by an enzyme preparation of red campion (Silene dioica (L) Clairv) leaves. FEBS Lett. 91 (1978) 281-284. [PMID: 680134]
Accepted name: trans-L-3-hydroxyproline dehydratase
Reaction: trans-L-3-hydroxyproline = Δ1-pyrroline 2-carboxylate + H2O
Other name(s): trans-L-3-hydroxyproline hydro-lyase
Systematic name: trans-L-3-hydroxyproline hydro-lyase (Δ1-pyrroline-2-carboxylate-forming)
Comments: Highly specific. 2,3-Dehydroproline is an intermediate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Ramaswamy, S.G. Conversion of 3-hydroxyproline to proline in the rat requires reduced pyridine-nucleotides. Fed. Proc. 42 (1983) 2232 only.
[EC 4.2.1.78 Transferred entry: (S)-norcoclaurine synthase. Now EC 3.5.99.14, (S)-norcoclaurine synthase (EC 4.2.1.78 created 1984, modified 1999, deleted 2024)]
Accepted name: 2-methylcitrate dehydratase
Reaction: (2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate = (Z)-but-2-ene-1,2,3-tricarboxylate + H2O
Glossary: (2S,3S)-2-methylcitrate = (2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate
cis-2-methylaconitate = (Z)-but-2-ene-1,2,3-tricarboxylate
Other name(s): 2-methylcitrate hydro-lyase; PrpD; 2-hydroxybutane-1,2,3-tricarboxylate hydro-lyase
Systematic name: (2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate hydro-lyase [(Z)-but-2-ene-1,2,3-tricarboxylate-forming]
Comments: The enzyme is specific for (2S,3S)-methylcitrate, showing no activity with (2R,3S)-methylcitrate [2]. The enzyme can also use cis-aconitate as a substrate but more slowly [2]. Both this enzyme and EC 4.2.1.3, aconitate hydratase, are required to complete the isomerization of (2S,3S)-methylcitrate to (2R,3S)-2-methylisocitrate [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 80891-26-5
References:
1. Aoki, H. and Tabuchi, T. Purification and properties of 2-methylcitrate dehydratase from Yarrowia lipolytica. Agric. Biol. Chem. 45 (1981) 2831-2837.
2. Brock, M., Maerker, C., Schütz, A., Völker, U. and Buckel, W. Oxidation of propionate to pyruvate in Escherichia coli. Involvement of methylcitrate dehydratase and aconitase. Eur. J. Biochem. 269 (2002) 6184-6194. [PMID: 12473114]
Accepted name: 2-oxopent-4-enoate hydratase
Reaction: 4-hydroxy-2-oxopentanoate = 2-oxopent-4-enoate + H2O
For diagram of reaction click here and another click here and another.
Other name(s): 2-keto-4-pentenoate hydratase; OEH; 2-keto-4-pentenoate (vinylpyruvate) hydratase; 4-hydroxy-2-oxopentanoate hydro-lyase
Systematic name: 4-hydroxy-2-oxopentanoate hydro-lyase (2-oxopent-4-enoate-forming)
Comments: Also acts, more slowly, on cis-2-oxohex-4-enoate, but not on the trans-isomer.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 64427-80-1
References:
1. Kunz, D.A., Ribbons, D.W. and Chapman, P.J. Metabolism of allylglycine and cis-crotylglycine by Pseudomonas putida (arvilla) mt-2 harboring a TOL plasmid. J. Bacteriol. 148 (1981) 72-82. [PMID: 7287632]
Accepted name: D(–)-tartrate dehydratase
Reaction: (S,S)-tartrate = oxaloacetate + H2O
Other name(s): D-tartrate dehydratase; (S,S)-tartrate hydro-lyase
Systematic name: (S,S)-tartrate hydro-lyase (oxaloacetate-forming)
Comments: Requires Fe2+ or Mn2+. cf. EC 4.2.1.32 L(+)-tartrate dehydratase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 82532-88-5
References:
1. Rode, H. and Giffhorn, F. D-(–)-Tartrate dehydratase of Rhodopseudomonas sphaeroides: purification, characterization, and application to enzymatic determination of D-(–)-tartrate.J. Bacteriol. 150 (1982) 1061-1068. [PMID: 6978882]
2. Rode, H. and Giffhorn, F. Ferrous- or cobalt ion-dependent D-(–)-tartrate dehydratase of pseudomonads: purification and properties. J. Bacteriol. 151 (1982) 1602-1604. [PMID: 7107563]
Accepted name: xylonate dehydratase
Reaction: D-xylonate = 2-dehydro-3-deoxy-D-arabinonate + H2O
Glossary: 2-dehydro-3-deoxy-D-arabinonate = 2-dehydro-3-deoxy-D-xylonate = 3-deoxy-L-glycero-pent-2-ulonate
Other name(s): D-xylo-aldonate dehydratase; D-xylonate dehydratase; D-xylonate hydro-lyase
Systematic name: D-xylonate hydro-lyase (2-dehydro-3-deoxy-D-arabinonate-forming)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 84788-77-2
References:
1. Dahms, A.S. and Donald, A. D-xylo-Aldonate dehydratase. Methods Enzymol. 90 (1982) 302-305. [PMID: 7154961]
2. Donald, A. Sibley, D., Lyons, D.E. and Dahms, A.S. D-Galactonate dehydrase. Purification and properties. J. Biol. Chem. 254 (1979) 2132-2137. [PMID: 422572]
Accepted name: 4-oxalomesaconate hydratase
Reaction: 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate = (1E,3E)-4-hydroxybuta-1,3-diene-1,2,4-tricarboxylate + H2O
For diagram of reaction click here.
Other name(s): 4-carboxy-2-oxohexenedioate hydratase; 4-carboxy-2-oxobutane-1,2,4-tricarboxylate 2,3-hydro-lyase; oxalmesaconate hydratase; γ-oxalmesaconate hydratase; 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate 2,3-hydro-lyase; LigJ; GalB; 4-oxalmesaconate hydratase
Systematic name: (1E,3E)-4-hydroxybuta-1,3-diene-1,2,4-tricarboxylate 1,2-hydro-lyase (2-hydroxy-4-oxobutane-1,2,4-tricarboxylate-forming)
Comments: This enzyme participates in the degradation of 3,4-dihydroxybenzoate (via the meta-cleavage pathway), syringate and 3,4,5-trihydroxybenzoate, catalysing the reaction in the opposite direction [1-3]. It accepts the enol-form of 4-oxalomesaconate, 2-hydroxy-4-carboxy-hexa-2,4-dienedioate [4].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 85204-95-1
References:
1. Maruyama, K. Enzymes responsible for degradation of 4-oxalmesaconic acid in Pseudomonas ochraceae. J. Biochem. 93 (1983) 567-574. [PMID: 6841354]
2. Maruyama, K. Purification and properties of γ-oxalomesaconate hydratase from Pseudomonas ochraceae grown with phthalate. Biochem. Biophys. Res. Commun. 128 (1985) 271-277. [PMID: 3985968]
3. Hara, H., Masai, E., Katayama, Y. and Fukuda, M. The 4-oxalomesaconate hydratase gene, involved in the protocatechuate 4,5-cleavage pathway, is essential to vanillate and syringate degradation in Sphingomonas paucimobilis SYK-6. J. Bacteriol. 182 (2000) 6950-6957. [PMID: 11092855]
4. Nogales, J., Canales, A., Jimenez-Barbero, J., Serra, B., Pingarron, J.M., Garcia, J.L. and Diaz, E. Unravelling the gallic acid degradation pathway in bacteria: the gal cluster from Pseudomonas putida. Mol. Microbiol. 79 (2011) 359-374. [PMID: 21219457]
Accepted name: nitrile hydratase
Reaction: An aliphatic amide = a nitrile + H2O
Other name(s): nitrilase; 3-cyanopyridine hydratase; NHase; L-NHase; H-NHase; acrylonitrile hydratase; aliphatic nitrile hydratase
Systematic name: aliphatic-amide hydro-lyase (nitrile-forming)
Comments: Acts on short-chain aliphatic nitriles, converting them into the corresponding acid amides. Does not act on these amides or on aromatic nitriles. cf. EC 3.5.5.1 nitrilase.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 82391-37-5
References:
1. Asano, Y., Fujishiro, K., Tani, Y. and Yamada, H. Microbial degradation of nitrile compounds. 5. Aliphatic nitrile hydratase from Arthrobacter sp J-1. Purification and characterization. Agric. Biol. Chem. 46 (1982) 1165-1174.
Accepted name: dimethylmaleate hydratase
Reaction: (2R,3S)-2,3-dimethylmalate = dimethylmaleate + H2O
For diagram click here.
Other name(s): (2R,3S)-2,3-dimethylmalate hydro-lyase
Systematic name: (2R,3S)-2,3-dimethylmalate hydro-lyase (dimethylmaleate-forming)
Comments: Requires Fe2+. Inhibited by oxygen.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 93229-56-2
References:
1. Kollmann-Koch, A. and Eggerer, H. Nicotinic acid metabolism. Dimethylmaleate hydratase. Hoppe-Seyler's Z. Physiol. Chem. 365 (1984) 847-857. [PMID: 6489933]
[EC 4.2.1.86 Deleted entry: 16-dehydroprogesterone hydratase (reaction is identical to that of EC 4.2.1.98, 16α-hydroxyprogesterone dehydratase) (EC 4.2.1.86 created 1989, deleted 2004)]
Accepted name: octopamine dehydratase
Reaction: 1-(4-hydroxyphenyl)-2-aminoethanol = (4-hydroxyphenyl)acetaldehyde + NH3
Other name(s): octopamine hydrolyase; octopamine hydro-lyase (deaminating)
Systematic name: 1-(4-hydroxyphenyl)-2-aminoethanol hydro-lyase [deaminating; (4-hydroxyphenyl)acetaldehyde-forming]
Comments: The enzyme-catalysed reaction is believed to be dehydration to an enamine, which is spontaneously hydrolysed to an aldehyde and ammonia.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 109456-55-5
References:
1. Cuskey, S.M., Peccoraro, V. and Olsen, R.H. Initial catabolism of aromatic biogenic amines by Pseudomonas aeruginosa PAO: pathway description, mapping of mutations, and cloning of essential genes. J. Bacteriol. 169 (1987) 2398-2404. [PMID: 3034855]
Accepted name: synephrine dehydratase
Reaction: (R)-synephrine = (4-hydroxyphenyl)acetaldehyde + methylamine
Glossary: (R)-synephrine = D-(–)-synephrine = 4-[(1R)-1-hydroxy-2-(methylamino)ethyl]phenol
Other name(s): syringinase
Systematic name: (R)-synephrine hydro-lyase (methylamine-forming)
Comments: Removal of H2O from (R)-synephrine produces a 2,3-enamine, which hydrolyses to the products shown in the reaction above. The enzyme from Arthrobacter synephrinum is highly specific [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 104118-54-9
References:
1. Veeraswamy, M., Devi, N.A., Krishnan Kutty, R. and Subba Rao, P.V. Conversion of (±) synephrine into p-hydroxyphenylacetaldehyde by Arthrobacter synephrinum. A novel enzymic reaction. Biochem. J. 159 (1976) 807-809. [PMID: 1008837]
2. Manne, V., Kutty, K.R. and Pillarisetti, S.R. Purification and properties of synephrinase from Arthrobacter synephrinum. Arch. Biochem. Biophys. 248 (1986) 324-334. [PMID: 3729420]
[EC 4.2.1.89 Deleted entry: carnitine dehydratase. The activity has now been shown to be due to EC 2.8.3.21, L-carnitine CoA-transferase and EC 4.2.1.149, crotonobetainyl-CoA hydratase. (EC 4.2.1.89 created 1989, deleted 2013)]
Accepted name: L-rhamnonate dehydratase
Reaction: L-rhamnonate = 2-dehydro-3-deoxy-L-rhamnonate + H2O
For diagram of reaction click here.
Other name(s): L-rhamnonate hydro-lyase
Systematic name: L-rhamnonate hydro-lyase (2-dehydro-3-deoxy-L-rhamnonate-forming)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 99533-47-8
References:
1. Rigo, L.U., Maréchal, L.R., Vieira, M.M. and Veiga, L.A. Oxidative pathway for L-rhamnose degradation in Pullularia pullulans. Can. J. Microbiol. 31 (1985) 817-822.
Accepted name: arogenate dehydratase
Reaction: L-arogenate = L-phenylalanine + H2O + CO2
For diagram click here.
Other name(s): carboxycyclohexadienyl dehydratase; L-arogenate hydro-lyase (decarboxylating)
Systematic name: L-arogenate hydro-lyase (decarboxylating; L-phenylalanine-forming)
Comments: Also acts on prephenate and D-prephenyllactate. cf. EC 4.2.1.51, prephenate dehydratase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 76600-70-9
References:
1. Fischer, R. and Jensen, R. Arogenate dehydratase. Methods Enzymol. 142 (1987) 495-502. [PMID: 3600377]
2. Zamir, L.O., Tiberio, R., Devor, K.A., Sauriol, F., Ahmad, S. and Jensen, R.A. Structure of D-prephenyllactate. A carboxycyclohexadienyl metabolite from Neurospora crassa. J. Biol. Chem. 263 (1988) 17284-17290. [PMID: 2972718]
3. Siehl, D.L. and Conn, E.E. Kinetic and regulatory properties of arogenate dehydratase in seedlings of Sorghum bicolor (L.) Moench. Arch. Biochem. Biophys. 260 (1988) 822-829. [PMID: 3124763]
Accepted name: hydroperoxide dehydratase
Reaction: (9Z,11E,15Z)-(13S)-hydroperoxyoctadeca-9,11,15-trienoate = (9Z,15Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate + H2O
Glossary: 13-hydroperoxylinolenoate = (9Z,11E,15Z)-(13S)-hydroperoxyoctadeca-9,11,15-trienoate
Other name(s): hydroperoxide isomerase; linoleate hydroperoxide isomerase; linoleic acid hydroperoxide isomerase; HPI; (9Z,11E,14Z)-(13S)-hydroperoxyoctadeca-9,11,14-trienoate 12,13-hydro-lyase; (9Z,11E,14Z)-(13S)-hydroperoxyoctadeca-9,11,14-trienoate 12,13-hydro-lyase [(9Z)-(13S)-12,13-epoxyoctadeca-9,11-dienoate-forming]; allene oxide synthase; AOS
Systematic name: (9Z,11E,15Z)-(13S)-hydroperoxyoctadeca-9,11,15-trienoate 12,13-hydro-lyase [(9Z,15Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate-forming]
Comments: Acts on a number of unsaturated fatty-acid hydroperoxides, forming the corresponding allene oxides. The product of the above reaction is unstable and is acted upon by EC 5.3.99.6, allene-oxide cyclase, to form the cyclopentenone derivative (15Z)-12-oxophyto-10,15-dienoate (OPDA), which is the first cyclic and biologically active metabolite in the jasmonate biosynthesis pathway [3]. The enzyme from many plants belongs to the CYP-74 family of P450 monooxygenases [4].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Esselman, W.J. and Clagett, C.O. Products of linoleic hydroperoxide-decomposing enzyme of alfalfa seed. J. Lipid Res. 15 (1974) 173-178. [PMID: 4208994]
2. Hamberg, M. Mechanism of corn hydroperoxide isomerase - detection of 12,13(S)-oxido-9(Z),11-octadecadienoic acid. Biochim. Biophys. Acta 920 (1987) 76-84.
3. Hamberg, M. Biosynthesis of 12-oxo-10,15(Z)-phytodienoic acid: identification of an allene oxide cyclase. Biochem. Biophys. Res. Commun. 156 (1988) 543-550. [PMID: 3178850]
4. Laudert, D., Pfannschmidt, U., Lottspeich, F., Holländer-Czytko, H. and Weiler, E.W. Cloning, molecular and functional characterization of Arabidopsis thaliana allene oxide synthase (CYP 74), the first enzyme of the octadecanoid pathway to jasmonates. Plant Mol. Biol. 31 (1996) 323-335. [PMID: 8756596]
Accepted name: ATP-dependent NAD(P)H-hydrate dehydratase
Reaction: (1) ATP + (6S)-6β-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide = ADP + phosphate + NADH
(2) ATP + (6S)-6β-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate = ADP + phosphate + NADPH
For diagram of reaction click here
Glossary: (6S)-6β-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide = (S)-NADH-hydrate = (S)-NADHX
(6S)-6β-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate = (S)-NADPH-hydrate = (S)-NADPHX
Other name(s): reduced nicotinamide adenine dinucleotide hydrate dehydratase; ATP-dependent H4NAD(P)+OH dehydratase; (6S)-β-6-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine-dinucleotide hydro-lyase(ATP-hydrolysing); (6S)-6-β-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine-dinucleotide hydro-lyase (ATP-hydrolysing; NADH-forming)
Systematic name: (6S)-6β-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine-dinucleotide hydro-lyase (ATP-hydrolysing; NADH-forming)
Comments: Acts equally well on hydrated NADH and hydrated NADPH. NAD(P)H spontaneously hydrates to both the (6S)- and (6R)- isomers, and these are interconverted by EC 5.1.99.6, NAD(P)H-hydrate epimerase, to a 60:40 ratio [4]. Hence EC 4.2.1.93 together with EC 5.1.99.6 can restore the mixture of hydrates into NAD(P)H [3,4]. The enzyme from eukaryotes has no activity with ADP, contrary to the enzyme from bacteria (cf. EC 4.2.1.136, ADP-dependent NAD(P)H-hydrate dehydratase) [4].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 116669-08-0
References:
1. Meinhart, J.O., Chaykin, S. and Krebs, E.G. Enzymatic conversion of a reduced diphosphopyridine nucleotide derivative to reduced diphosphopyridine nucleotide. J. Biol. Chem. 220 (1956) 821-829. [PMID: 13331940]
2. Regueiro Varela, B., Amelunxen, R. and Grisolia, S. Synthesis and degradation of monohydroxytetrahydronicotinamide adenine dinucleotide phosphate. Physiol. Chem. Phys. 2 (1970) 445-454.
3. Acheson, S.A., Kirkman, H.N. and Wolfenden, R. Equilibrium of 5,6-hydration of NADH and mechanism of ATP-dependent dehydration. Biochemistry 27 (1988) 7371-7375. [PMID: 3061454]
4. Marbaix, A.Y., Noel, G., Detroux, A.M., Vertommen, D., Van Schaftingen, E. and Linster, C.L. Extremely conserved ATP- or ADP-dependent enzymatic system for nicotinamide nucleotide repair. J. Biol. Chem. 286 (2011) 41246-41252. [PMID: 21994945]
Accepted name: scytalone dehydratase
Reaction: scytalone = 1,3,8-trihydroxynaphthalene + H2O
Other name(s): scytalone 7,8-hydro-lyase
Systematic name: scytalone 7,8-hydro-lyase (1,3,8-trihydroxynaphthalene-forming)
Comments: Involved, with EC 1.1.1.252 tetrahydroxynaphthalene reductase, in the biosynthesis of melanin in pathogenic fungi.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 118901-79-4
References:
1. Butler, M.J., Lazarovits, G., Higgins, V.J. and Lachance, M.-A. Partial-purification and characterization of a dehydratase associated with the pentaketide melanogenesis pathway of Phaeococcomyces sp and other fungi. Exp. Mycol. 12 (1988) 367-376.
2. Tajima, S., Kubo, Y., Furusawa, I. and Shishiyama, J. Purification of a melanin biosynthetic enzyme converting scytalone to 1,3,8-trihydroxynaphthalene from Cochliobolus miyabeanus. Exp. Mycol. 13 (1989) 69.
3. Wheeler, M.H. and Greenblatt, G.A. The inhibition of melanin biosynthetic reactions in Pyricularia oryzae by compounds that prevent rice blast disease. Exp. Mycol. 12 (1988) 151-160.
Accepted name: kievitone hydratase
Reaction: kievitone hydrate = kievitone + H2O
Other name(s): KHase; kievitone-hydrate hydro-lyase
Systematic name: kievitone-hydrate hydro-lyase (kievitone-forming)
Comments: The enzyme from Fusarium sp. hydrates the methylbutenyl sidechain of the isoflavonoid phytoalexins, thus reducing their toxicity.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 70431-10-6
References:
1. Turbek, C.S., Li, D., Choi, G.H., Schardl, C.L. and Smith, D.A. Induction and purification of kievitone hydratase from Fusarium solani f. sp. phaseoli. Phytochemistry 29 (1990) 2841-2846. [PMID: 1366757]
Accepted name: 4a-hydroxytetrahydrobiopterin dehydratase
Reaction: 4a-hydroxytetrahydrobiopterin = 6,7-dihydrobiopterin + H2O
For diagram of reactionclick here
Glossary: 4a-hydroxytetrahydrobiopterin = 6-[(1R,2S)-1,2-dihydroxypropyl]-5,6,7,8-tetrahydro-4a-hydroxypterin
6,7-dihydrobiopterin = 6-[(1R,2S)-1,2-dihydroxypropyl]-6,7-dihydropterin
Other name(s): 4α-hydroxy-tetrahydropterin dehydratase; 4a-carbinolamine dehydratase; pterin-4α-carbinolamine dehydratase; 4a-hydroxytetrahydrobiopterin hydro-lyase
Systematic name: a-hydroxytetrahydrobiopterin hydro-lyase (6,7-dihydrobiopterin-forming)
Comments: In concert with EC 1.5.1.34, 6,7-dihydropteridine reductase, the enzyme recycles 4a-hydroxytetrahydrobiopterin back to tetrahydrobiopterin, a cosubstrate for several enzymes, including aromatic amino acid hydroxylases. The enzyme is bifunctional, and also acts as a dimerization cofactor of hepatocyte nuclear factor-1α (HNF-1).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 87683-70-3
References:
1. Citron, B.A., Davis, M.D., Milstien, S., Gutierrez, J., Mendel, D.B., Crabtree, G.R. and Kaufman, S. Identity of 4a-carbinolamine dehydratase, a component of the phenylalanine hydroxylation system, and DCoH, a transregulator of homeodomain proteins. Proc. Natl. Acad. Sci. USA 89 (1992) 11891-11894. [PMID: 1465414]
2. Hauer, C.R., Rebrin, I., Thöny, B., Neuheiser, F., Curtius, H.C., Hunziker, P., Blau, N., Ghisla, S., Heizmann, C.W. Phenylalanine hydroxylase-stimulating protein: pterin-4α-carbinolamine dehydratase from rat and human liver. J. Biol. Chem. 268 (1993) 4828-4831. [PMID: 8444860]
3. Thony, B., Neuheiser, F., Blau, N. and Heizmann, C.W. Characterization of the human PCBD gene encoding the bifunctional protein pterin-4 α-carbinolamine dehydratase/dimerization cofactor for the transcription factor HNF-1 α. Biochem. Biophys. Res. Commun. 210 (1995) 966-973. [PMID: 7763270]
4. Endrizzi, J.A., Cronk, J.D., Wang, W., Crabtree, G.R. and Alber, T. Crystal structure of DCoH, a bifunctional, protein-binding transcriptional coactivator. Science 268 (1995) 556-559. [PMID: 7725101]
5. Cronk, J.D., Endrizzi, J.A. and Alber, T. High-resolution structures of the bifunctional enzyme and transcriptional coactivator DCoH and its complex with a product analogue. Protein Sci. 5 (1996) 1963-1972. [PMID: 8897596]
Accepted name: phaseollidin hydratase
Reaction: phaseollidin hydrate = phaseollidin + H2O
Other name(s): phaseollidin-hydrate hydro-lyase
Systematic name: phaseollidin-hydrate hydro-lyase (phaseollidin-forming)
Comments: the enzyme from Fusarium solani, which is distinct from kievitone hydratase (EC 4.2.1.95), hydrates the methylbutenyl side-chain of the isoflavonoid phytoalexin, phaseollidin.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 143597-34-6
References:
1. Turbek, C.S., Smith, D.A., Schardl, C.L. An extracellular enzyme from Fusarium solani f.sp. phaseoli, which catalyses hydration of the isoflavonoid phytoalexin, phaseollidin. FEMS Microbiol. Lett. 94 (1992) 187-190. [PMID: 1521768]
Accepted name: 16α-hydroxyprogesterone dehydratase
Reaction: 16α-hydroxyprogesterone = 16,17-didehydroprogesterone + H2O
For diagram click here.
Other name(s): hydroxyprogesterone dehydroxylase; 16α-hydroxyprogesterone dehydroxylase; 16α-dehydroxylase; 16α-hydroxyprogesterone hydro-lyase
Systematic name: 16α-hydroxyprogesterone hydro-lyase (16,17-didehydroprogesterone-forming)
Comments: 16α-Hydroxypregnenolone is also a substrate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 89287-36-5
References:
1. Glass, T.L. and Lamppa, R.S. Purification and properties of 16α-hydroxyprogesterone dehydroxylase from Eubacterium sp. strain 144. Biochim. Biophys. Acta 837 (1985) 103-110. [PMID: 4052439]
Accepted name: 2-methylisocitrate dehydratase
Reaction: (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = (Z)-but-2-ene-1,2,3-tricarboxylate + H2O
Glossary: cis-2-methylaconitate = (Z)-but-2-ene-1,2,3-tricarboxylate
(2S,3R)-2-methylisocitrate = (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = threo-Ds-2-methylisocitrate
Other name(s): (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate hydro-lyase
Systematic name: (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate hydro-lyase [(Z)-but-2-ene-1,2,3-tricarboxylate-forming]
Comments: The enzyme from the fungus Yarrowia lipolytica (Saccharomycopsis) does not act on isocitrate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 170780-51-5
References:
1. Aoki, H., Uchiyama, H., Umetsu, H., Tabuchi, T. Isolation of 2-methylisocitrate dehydratase, a new enzyme serving in the methylcitric acid cycle for propionate metabolism, from Yarrowia lipolytica. Biosci. Biotechnol. Biochem. 59 (1995) 1825-1828
2. Tabuchi, T., Umetsu, H., Aoki, H., Uchiyama, H. Characteristics of 2-methylisocitrate dehydratase, isolated from Yarrowia lipolytica, in comparison to aconitase. Biosci. Biotechnol. Biochem. 59 (1995) 2013-2017.
Accepted name: cyclohexa-1,5-dienecarbonyl-CoA hydratase
Reaction: 6-hydroxycyclohex-1-ene-1-carbonyl-CoA = cyclohexa-1,5-diene-1-carbonyl-CoA + H2O
For diagram of reaction click here.
Other name(s): cyclohexa-1,5-diene-1-carbonyl-CoA hydratase; dienoyl-CoA hydratase; cyclohexa-1,5-dienecarbonyl-CoA hydro-lyase (incorrect)
Systematic name: 6-hydroxycyclohex-1-ene-1-carbonyl-CoA hydro-lyase (cyclohexa-1,5-diene-1-carbonyl-CoA-forming)
Comments: Forms part of the anaerobic benzoate degradation pathway, which also includes EC 1.3.8.6 (glutaryl-CoA dehydrogenase), EC 1.3.7.8 (benzoyl-CoA reductase) and EC 4.2.1.55 (3-hydroyxbutyryl-CoA dehydratase).
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, CAS registry number: 214355-79-0
References:
1. Laempe, D., Eisenreich, W., Bacher, A. and Fuchs, G. Cyclohexa-1,5-diene-1-carboxyl-CoA hydratase, an enzyme involved in anaerobic metabolism of benzoyl-CoA in the denitrifying bacterium Thauera aromatica. Eur. J. Biochem. 255 (1998) 618-627. [PMID: 9738901] [Erratum Eur. J. Biochem. 257 (1998) 528 only]
2. Harwood, C.S. and Gibson, J. Shedding light on anaerobic benzene ring degradation: a process unique to prokaryotes? J. Bacteriol. 179 (1997) 301-309. [PMID: 8990279]
3. Koch, J., Eisenreich, W., Bacher, A. and Fuchs, G. Products of enzymatic reduction of benzoyl-CoA, a key reaction in anaerobic aromatic metabolism. Eur. J. Biochem. 211 (1993) 649-661. [PMID: 8436125]