4)-β-D-xylopyranosyl-(14)-β-D-xylopyranose reducing-end xylanase
An asterisk before 'EC' indicates that this is an amendment to an existing enzyme rather than a new enzyme entry.
Common name: 3"-deamino-3"-oxonicotianamine reductase
Reaction: 2'-deoxymugineic acid + NAD(P)+ = 3"-deamino-3"-oxonicotianamine + NAD(P)H + H+
For diagram click here.
Systematic name: 2'-deoxymugineic acid:NAD(P)+ 3"-oxidoreductase
References:
1. Shojima, S., Nishizawa, N.-K., Fushiya, S., Nozoe, S., Irifune, T. and Mori, S. In vitro biosynthesis of 2'-deoxymugineic acid from L-methionine and nicotianamine. Plant Physiol. 93 (1990) 1497-1503.
Common name: arogenate dehydrogenase
Reaction: L-arogenate + NAD+ = L-tyrosine + NADH + CO2
For diagram click here.
Other name(s): arogenic dehydrogenase (ambiguous); cyclohexadienyl dehydrogenase; pretyrosine dehydrogenase (ambiguous); L-arogenate:NAD+ oxidoreductase
Systematic name: L-arogenate:NAD+ oxidoreductase (decarboxylating)
Comments: See also EC 1.3.1.12 (prephenate dehydrogenase), EC 1.3.1.78 [arogenate dehydrogenase (NADP+)] and EC 1.3.1.79 (arogenate dehydrogenase [NAD(P)+]).
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 64295-75-6
References:
1. Stenmark, S.L., Pierson, D.L., Jensen, R.A. and Glover, G.I. Blue-green bacteria synthesise L-tyrosine by the pretyrosine pathway. Nature 247 (1974) 290-292. [PMID: 4206476]
2. Byng, G., Whitaker, R., Flick, C. and Jensen, R.A. Enzymology of L-tyrosine biosynthesis in corn (Zea mays). Phytochemistry 20 (1981) 1289-1292.
3. Mayer, E., Waldner-Sander, S., Keller, B., Keller, E. and Lingens, F. Purification of arogenate dehydrogenase from Phenylobacterium immobile. FEBS Lett. 179 (1985) 208-212. [PMID: 3967752]
4. Lingens, F., Keller, E. and Keller, B. Arogenate dehydrogenase from Phenylobacterium immobile. Methods Enzymol. 142 (1987) 513-518.
5. 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]
Common name: arogenate dehydrogenase (NADP+)
Reaction: L-arogenate + NADP+ = L-tyrosine + NADPH + CO2
For diagram click here.
Other name(s): arogenic dehydrogenase (ambiguous); pretyrosine dehydrogenase (ambiguous); TyrAAT1; TyrAAT2; TyrAa
Systematic name: L-arogenate:NADP+ oxidoreductase (decarboxylating)
Comments: Unlike EC 1.3.1.43 [arogenate dehydrogenase (NAD+)] and EC 1.3.1.79 [arogenate dehydrogenase (NAD(P)+)], this enzyme has a strict requirement for NADP+. The enzyme from Synechocystis sp. PCC 6803 and the isoform TyrAAT1 cannot use prephenate as a substrate, while the isoform TyrAAT2 can use it only very poorly [3,4].
Links to other databases: CAS registry number: 64295-75-6
References:
1. Byng, G., Whitaker, R., Flick, C. and Jensen, R.A. Enzymology of L-tyrosine biosynthesis in corn (Zea mays). Phytochemistry 20 (1981) 1289-1292.
2. Gaines, C.G., Byng, G.S., Whitaker, R.J. and Jensen, R.A. L-Tyrosine regulation and biosynthesis via arogenate dehydrogenase in suspension-cultured cells of Nicotiana silvestris Speg. et Comes. Planta 156 (1982) 233-240.
3. Rippert, P. and Matringe, M. Purification and kinetic analysis of the two recombinant arogenate dehydrogenase isoforms of Arabidopsis thaliana. Eur. J. Biochem. 269 (2002) 4753-4761. [PMID: 12354100]
4. Bonner, C.A., Jensen, R.A., Gander, J.E. and Keyhani, N.O. A core catalytic domain of the TyrA protein family: arogenate dehydrogenase from Synechocystis. Biochem. J. 382 (2004) 279-291. [PMID: 15171683]
Common name: arogenate dehydrogenase [NAD(P)+]
Reaction: L-arogenate + NAD(P)+ = L-tyrosine + NAD(P)H + CO2
For diagram click here.
Other name(s): arogenic dehydrogenase (ambiguous); cyclohexadienyl dehydrogenase; pretyrosine dehydrogenase (ambiguous)
Systematic name: L-arogenate:NAD(P)+ oxidoreductase (decarboxylating)
Comments: See also EC 1.3.1.12 (prephenate dehydrogenase), EC 1.3.1.43 [arogenate dehydrogenase (NAD+)], and EC 1.3.1.78 [arogenate dehydrogenase (NADP+)].
Links to other databases: CAS registry number: 64295-75-6
References:
1. Connelly, J.A. and Conn, E.E. Tyrosine biosynthesis in Sorghum bicolor: isolation and regulatory properties of arogenate dehydrogenase. Z. Naturforsch. [C] 41 (1986) 69-78. [PMID: 2939643]
2. Bonner, C. and Jensen, R. Arogenate dehydrogenase. Methods Enzymol. 142 (1987) 488-494. [PMID: 3600376]
Common name: pyrroloquinoline-quinone synthase
Reaction: 6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,5,6,7,8-octahydroquinoline-2,4-dicarboxylate + 3 O2 = 4,5-dioxo-3a,4,5,6,7,8,9,9b-octahydro-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylate + 2 H2O2 + 2 H2O
For diagram click here.
Other name(s): PqqC
Systematic name: 6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,5,6,7,8-octahydroquinoline-2,4-dicarboxylate:oxygen oxidoreductase (cyclizing)
Comments: So far only a single turnover of the enzyme has been observed, and the pyrroloquinoline quinone remains bound to it. It is not yet known what releases the product in the bacterium.
References:
1. Magnusson, O.T., Toyama, H., Saeki, M., Schwarzenbacher, R. and Klinman, J.P. The structure of a biosynthetic intermediate of pyrroloquinoline quinone (PQQ) and elucidation of the final step of PQQ biosynthesis. J. Am. Chem. Soc. 126 (2004) 5342-5343. [PMID: 15113189]
2. Magnusson, O.T., Toyama, H., Saeki, M., Rojas, A., Reed, J.C., Liddington, R.C., Klinman, J.P. and Schwarzenbacher, R. Quinone biogenesis: Structure and mechanism of PqqC, the final catalyst in the production of pyrroloquinoline quinone. Proc. Natl. Acad. Sci. USA 101 (2004) 7913-7918. [PMID: 15148379]
3. Toyama, H., Chistoserdova, L. and Lidstrom, M.E. Sequence analysis of pqq genes required for biosynthesis of pyrroloquinoline quinone in Methylobacterium extorquens AM1 and the purification of a biosynthetic intermediate. Microbiology 143 (1997) 595-602. [PMID: 9043136]
4. Toyama, H., Fukumoto, H., Saeki, M., Matsushita, K., Adachi, O. and Lidstrom, M.E. PqqC/D, which converts a biosynthetic intermediate to pyrroloquinoline quinone. Biochem. Biophys. Res. Commun. 299 (2002) 268-272. [PMID: 1243798]
5. Schwarzenbacher, R., Stenner-Liewen, F., Liewen, H., Reed, J.C. and Liddington, R.C. Crystal structure of PqqC from Klebsiella pneumoniae at 2.1 Å resolution. Protein 56 (2004) 401-403. [PMID: 15211525]
Common name: NAD(P)H dehydrogenase (quinone)
Reaction: NAD(P)H + H+ + a quinone = NAD(P)+ + a hydroquinone
Other name(s): menadione reductase; phylloquinone reductase; quinone reductase; dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate, quinone); DT-diaphorase; flavoprotein NAD(P)H-quinone reductase; menadione oxidoreductase; NAD(P)H dehydrogenase; NAD(P)H menadione reductase; NAD(P)H-quinone dehydrogenase; NAD(P)H-quinone oxidoreductase; NAD(P)H: (quinone-acceptor)oxidoreductase; NAD(P)H: menadione oxidoreductase; NADH-menadione reductase; naphthoquinone reductase; p-benzoquinone reductase; reduced NAD(P)H dehydrogenase; viologen accepting pyridine nucleotide oxidoreductase; vitamin K reductase; diaphorase; reduced nicotinamide-adenine dinucleotide (phosphate) dehydrogenase; vitamin-K reductase; NAD(P)H2 dehydrogenase (quinone); NQO1; QR1; NAD(P)H:(quinone-acceptor) oxidoreductase
Systematic name: NAD(P)H:quinone oxidoreductase
Comments: A flavoprotein. The enzyme catalyses a two-electron reduction and has a preference for short-chain acceptor quinones, such as ubiquinone, benzoquinone, juglone and duroquinone [6]. The animal, but not the plant, form of the enzyme is inhibited by dicoumarol.
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, PDB, CAS registry number: 9032-20-6
References:
1. di Prisco, G., Casola, L. and Giuditta, A. Purification and properties of a soluble reduced nicotinamide-adenine dinucleotide (phosphate) dehydrogenase from the hepatopancreas of Octopus vulgaris. Biochem. J. 105 (1967) 455-460. [PMID: 4171422]
2. Giuditta, A. and Strecker, H.J. Purification and some properties of a brain diaphorase. Biochim. Biophys. Acta 48 (1961) 10-19. [PMID: 13705804]
3. Märki, F. and Martius, C. Vitamin K-Reductase, Darsellung und Eigenschaften. Biochem. Z. 333 (1960) 111-135. [PMID: 13765127]
4. Misaka, E. and Nakanishi, K. Studies on menadione reductase of bakers' yeast. I. Purification, crystallization and some properties. J. Biochem. (Tokyo) 53 (1963) 465-471.
5. Wosilait, W.D. The reduction of vitamin K1 by an enzyme from dog liver. J. Biol. Chem. 235 (1960) 1196-1201. [PMID: 13846011]
6. Sparla, F., Tedeschi, G. and Trost, P. NAD(P)H:(quinone-acceptor) oxidoreductase of tobacco leaves is a flavin mononucleotide-containing flavoenzyme. Plant Physiol. 112 (1996) 249-258. [PMID: 12226388]
7. Braun, M., Bungert, S. and Friedrich, T. Characterization of the overproduced NADH dehydrogenase fragment of the NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli. Biochemistry 37 (1998) 1861-1867. [PMID: 9485311]
8. Jaiswal, A.K. Characterization and partial purification of microsomal NAD(P)H:quinone oxidoreductases. Arch. Biochem. Biophys. 375 (2000) 62-68. [PMID: 10683249]
9. Li, R., Bianchet, M.A., Talalay, P. and Amzel, L.M. The three-dimensional structure of NAD(P)H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: mechanism of the two-electron reduction. Proc. Natl. Acad. Sci. USA 92 (1995) 8846-8850. [PMID: 7568029]
[EC 1.6.99.2 Transferred entry: now EC 1.6.5.2, NAD(P)H dehydrogenase (quinone). The enzyme was erroneously transferred from this sub-subclass in 1965 (EC 1.6.99.2 created 1961 as EC 1.6.5.2, transferred 1965 to EC 1.6.99.2, deleted 2005)]
Common name: ribosyldihydronicotinamide dehydrogenase (quinone)
Reaction: 1-(β-D-ribofuranosyl)-1,4-dihydronicotinamide + a quinone = 1-(β-D-ribofuranosyl)nicotinamide + a hydroquinone
For diagram click here.
Other name(s): NRH:quinone oxidoreductase 2; NQO2; NQO2; NAD(P)H:quinone oxidoreductase-2 (misleading); QR2; quinone reductase 2; N-ribosyldihydronicotinamide dehydrogenase (quinone); NAD(P)H:quinone oxidoreductase2 (misleading)
Systematic name: 1-(β-D-ribofuranosyl)-1,4-dihydronicotinamide:quinone oxidoreductase
Comments: A flavoprotein. Unlike EC 1.6.5.8, NAD(P)H dehydrogenase (quinone), this quinone reductase cannot use NADH or NADPH; instead it uses N-ribosyl- and N-alkyldihydronicotinamides. Polycyclic aromatic hydrocarbons, such as benz[a]anthracene, and the oestrogens 17β-estradiol and diethylstilbestrol are potent inhibitors, but dicoumarol is only a very weak inhibitor [2]. This enzyme can catalyse both 2-electron and 4-electron reductions, but one-electron acceptors, such as potassium ferricyanide, cannot be reduced [3].
References:
1. Liao, S., Dulaney, J.T. and Williams-Ashman, H.G. Purification and properties of a flavoprotein catalyzing the oxidation of reduced ribosyl nicotinamide. J. Biol. Chem. 237 (1962) 2981-2987. [PMID: 14465018]
2. Zhao, Q., Yang, X.L., Holtzclaw, W.D. and Talalay, P. Unexpected genetic and structural relationships of a long-forgotten flavoenzyme to NAD(P)H:quinone reductase (DT-diaphorase). Proc. Natl. Acad. Sci. USA 94 (1997) 1669-1674. [PMID: 9050836]
3. Wu, K., Knox, R., Sun, X.Z., Joseph, P., Jaiswal, A.K., Zhang, D., Deng, P.S. and Chen, S. Catalytic properties of NAD(P)H:quinone oxidoreductase-2 (NQO2), a dihydronicotinamide riboside dependent oxidoreductase. Arch. Biochem. Biophys. 347 (1997) 221-228. [PMID: 9367528]
4. Jaiswal, A.K. Human NAD(P)H:quinone oxidoreductase2. Gene structure, activity, and tissue-specific expression. J. Biol. Chem. 269 (1994) 14502-14508. [PMID: 8182056]
Common name: violaxanthin de-epoxidase
Reaction: (1) violaxanthin + ascorbate = antheraxanthin + dehydroascorbate + H2O
(2) antheraxanthin + ascorbate = zeaxanthin + dehydroascorbate + H2O
For diagram click here.
Other name(s): VDE
Systematic name: violaxanthin:ascorbate oxidoreductase
Comments: Along with EC 1.14.13.54, zeaxanthin epoxidase, this enzyme forms part of the xanthophyll (or violaxanthin) cycle for controlling the concentration of zeaxanthin in chloroplasts. It is activated by a low pH of the thylakoid lumen (produced by high light intensity). Zeaxanthin induces the dissipation of excitation energy in the chlorophyll of the light-harvesting protein complex of photosystem II. In higher plants the enzyme reacts with all-trans-diepoxides, such as violaxanthin, and all-trans-monoepoxides, but in the alga Mantoniella squamata, only the diepoxides are good substrates.
References:
1. Yamamoto, H.Y. and Higashi, R.M. Violaxanthin de-epoxidase. Lipid composition and substrate specificity. Arch. Biochem. Biophys. 190 (1978) 514-522. [PMID: 102251]
2. Rockholm, D.C. and Yamamoto, H.Y. Violaxanthin de-epoxidase. Plant Physiol. 110 (1996) 697-703. [PMID: 8742341]
3. Bugos, R.C., Hieber, A.D. and Yamamoto, H.Y. Xanthophyll cycle enzymes are members of the lipocalin family, the first identified from plants. J. Biol. Chem. 273 (1998) 15321-15324. [PMID: 9624110]
4. Kuwabara, T., Hasegawa, M., Kawano, M. and Takaichi, S. Characterization of violaxanthin de-epoxidase purified in the presence of Tween 20: effects of dithiothreitol and pepstatin A. Plant Cell Physiol. 40 (1999) 1119-1126. [PMID: 10635115]
5. Latowski, D., Kruk, J., Burda, K., Skrzynecka-Jaskierm, M., Kostecka-Gugala, A. and Strzalka, K. Kinetics of violaxanthin de-epoxidation by violaxanthin de-epoxidase, a xanthophyll cycle enzyme, is regulated by membrane fluidity in model lipid bilayers. Eur. J. Biochem. 269 (2002) 4656-4665. [PMID: 12230579]
6. Goss, R. Substrate specificity of the violaxanthin de-epoxidase of the primitive green alga Mantoniella squamata (Prasinophyceae). Planta 217 (2003) 801-812. [PMID: 12748855]
7. Latowski, D., Akerlund, H.E. and Strzalka, K. Violaxanthin de-epoxidase, the xanthophyll cycle enzyme, requires lipid inverted hexagonal structures for its activity. Biochemistry 43 (2004) 4417-4420. [PMID: 15078086]
Common name: 2'-deoxymugineic-acid 2'-dioxygenase
Reaction: 2'-deoxymugineic acid + 2-oxoglutarate + O2 = mugineic acid + succinate + CO2
For diagram click here.
Other name(s): IDS3
Systematic name: 2'-deoxymugineic acid,2-oxoglutarate:oxygen oxidoreductase (2-hydroxylating)
Comments: Requires iron(II). It is also likely that this enzyme can catalyse the hydroxylation of 3-epihydroxy-2'-deoxymugineic acid to form 3-epihydroxymugineic acid.
References:
1. Nakanishi, H., Yamaguchi, H., Sasakuma, T., Nishizawa, N.K. and Mori, S. Two dioxygenase genes, Ids3 and Ids2, from Hordeum vulgare are involved in the biosynthesis of mugineic acid family phytosiderophores. Plant Mol. Biol. 44 (2000) 199-207. [PMID: 11117263]
2. Kobayashi, T., Nakanishi, H., Takahashi, M., Kawasaki, S., Nishizawa, N.K. and Mori, S. In vivo evidence that Ids3 from Hordeum vulgare encodes a dioxygenase that converts 2'-deoxymugineic acid to mugineic acid in transgenic rice. Planta 212 (2001) 864-871. [PMID: 11346963]
Common name: mugineic-acid 3-dioxygenase
Reaction: (1) mugineic acid + 2-oxoglutarate + O2 = 3-epihydroxymugineic acid + succinate + CO2
(2) 2'-deoxymugineic acid + 2-oxoglutarate + O2 = 3-epihydroxy-2'-deoxymugineic acid + succinate + CO2
For diagram click here.
Other name(s): IDS2
Systematic name: mugineic acid,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Comments: Requires iron(II).
References:
1. Nakanishi, H., Yamaguchi, H., Sasakuma, T., Nishizawa, N.K. and Mori, S. Two dioxygenase genes, Ids3 and Ids2, from Hordeum vulgare are involved in the biosynthesis of mugineic acid family phytosiderophores. Plant Mol. Biol. 44 (2000) 199-207. [PMID: 11117263]
2. Okumura, N., Nishizawa, N.K., Umehara, Y., Ohata, T., Nakanishi, H., Yamaguchi, T., Chino, M. and Mori. S. A dioxygenase gene (Ids2) expressed under iron deficiency conditions in the roots of Hordeum vulgare. Plant Mol. Biol. 25 (1994) 705-719. [PMID: 8061321]
Common name: 4'-methoxyisoflavone 2'-hydroxylase
Reaction: formononetin + NADPH + H+ + O2 = 2'-hydroxyformononetin + NADP+ + H2O
For diagram click here.
Other name(s): isoflavone 2'-monooxygenase (ambiguous); isoflavone 2'-hydroxylase (ambiguous)
Systematic name: formononetin,NADPH:oxygen oxidoreductase (2'-hydroxylating)
Comments: A heme-thiolate protein (P-450). Acts on isoflavones with a 4'-methoxy group, such as formononetin and biochanin A. Involved in the biosynthesis of the pterocarpin phytoalexins medicarpin and maackiain. EC 1.14.13.89, isoflavone 2'-hydroxylase, is less specific and acts on other isoflavones as well as 4'-methoxyisoflavones.
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 110183-49-8
References:
1. Hinderer, W., Flentje, U. and Barz, W. Microsomal isoflavone 2'-hydroxylases and 3'-hydroxylases from chickpea (Cicer arietinum L) cell-suspensions induced for pterocarpan phytoalexin formation. FEBS Lett. 214 (1987) 101-106.
Common name: isoflavone 2'-hydroxylase
Reaction: an isoflavone + NADPH + H+ + O2 = a 2'-hydroxyisoflavone + NADP+ + H2O
For diagram click here.
Other name(s): isoflavone 2'-monooxygenase; CYP81E1; CYP Ge-3
Systematic name: isoflavone,NADPH:oxygen oxidoreductase (2'-hydroxylating)
Comments: A heme-thiolate protein (P-450). Acts on daidzein, formononetin and genistein. EC 1.14.13.53, 4'-methoxyisoflavone 2'-hydroxylase, has the same reaction but is more specific as it requires a 4'-methoxyisoflavone.
References:
1. Akashi, T., Aoki, T. and Ayabe, S.-I. CYP81E1, a cytochrome P450 cDNA of licorice (Glycyrrhiza echinata L.), encodes isoflavone 2'-hydroxylase. Biochem. Biophys. Res. Commun. 251 (1998) 67-70. [PMID: 9790908]
Common name: zeaxanthin epoxidase
Reaction: (1) zeaxanthin + NAD(P)H + H+ + O2 = antheraxanthin + NAD(P)+ + H2O
(2) antheraxanthin + NAD(P)H + H+ + O2 = violaxanthin + NAD(P)+ + H2O
For diagram click here.
Other name(s): Zea-epoxidase
Systematic name: zeaxanthin,NAD(P)H:oxygen oxidoreductase
Comments: A flavoprotein (FAD) that is active under conditions of low light. Along with EC 1.10.99.2, violaxanthin de-epoxidase, this enzyme forms part of the xanthophyll (or violaxanthin) cycle, which is involved in protecting the plant against damage by excess light. It will also epoxidize lutein in some higher-plant species.
References:
1. Buch, K., Stransky, H. and Hager, A. FAD is a further essential cofactor of the NAD(P)H and O2-dependent zeaxanthin-epoxidase. FEBS Lett. 376 (1995) 45-48. [PMID: 8521963]
2. Bugos, R.C., Hieber, A.D. and Yamamoto, H.Y. Xanthophyll cycle enzymes are members of the lipocalin family, the first identified from plants. J. Biol. Chem. 273 (1998) 15321-15324. [PMID: 9624110]
3. Thompson, A.J., Jackson, A.C., Parker, R.A., Morpeth, D.R., Burbidge, A. and Taylor, I.B. Abscisic acid biosynthesis in tomato: regulation of zeaxanthin epoxidase and 9-cis-epoxycarotenoid dioxygenase mRNAs by light/dark cycles, water stress and abscisic acid. Plant Mol. Biol. 42 (2000) 833-845. [PMID: 10890531]
4. Hieber, A.D., Bugos, R.C. and Yamamoto, H.Y. Plant lipocalins: violaxanthin de-epoxidase and zeaxanthin epoxidase. Biochim. Biophys. Acta 1482 (2000) 84-91. [PMID: 11058750]
5. Frommolt, R., Goss, R. and Wilhelm, C. The de-epoxidase and epoxidase reactions of Mantoniella squamata (Prasinophyceae) exhibit different substrate-specific reaction kinetics compared to spinach. Planta 213 (2001) 446-456. [PMID: 11506368]
6. Frommolt, R., Goss, R. and Wilhelm, C. Erratum Report. The de-epoxidase and epoxidase reactions of Mantoniella squamata (Prasinophyceae) exhibit different substrate-specific reaction kinetics compared to spinach. Planta 213 (2001) 492. [PMID: 11506368]
7. Matsubara, S., Morosinotto, T., Bassi, R., Christian, A.L., Fischer-Schliebs, E., Luttge, U., Orthen, B., Franco, A.C., Scarano, F.R., Forster, B., Pogson, B.J. and Osmond, C.B. Occurrence of the lutein-epoxide cycle in mistletoes of the Loranthaceae and Viscaceae. Planta 217 (2003) 868-879. [PMID: 12844265]
Common name: deoxysarpagine hydroxylase
Reaction: 10-deoxysarpagine + NADPH + H+ + O2 = sarpagine + NADP+ + H2O
For diagram click here.
Other name(s): DOSH
Systematic name: 10-deoxysarpagine,NADPH:oxygen oxidoreductase (10-hydroxylating)
Comments: A heme-thiolate protein (P-450).
References:
1. Yu, B., Ruppert, M. and Stöckigt, J. Deoxysarpagine hydroxylase — a novel enzyme closing a short side pathway of alkaloid biosynthesis in Rauvolfia. Bioorg. Med. Chem. 10 (2002) 2479-2483. [PMID: 12057637]
Common name: phenylacetone monooxygenase
Reaction: phenylacetone + NADPH + H+ + O2 = benzyl acetate + NADP+ + H2O
For diagram click here.
Other name(s): PAMO
Systematic name: phenylacetone,NADPH:oxygen oxidoreductase
Comments: A flavoprotein (FAD). NADH cannot replace NADPH as coenzyme. In addition to phenylacetone, which is the best substrate found to date, this Baeyer-Villiger monooxygenase can oxidize other aromatic ketones [1-(4-hydroxyphenyl)propan-2-one, 1-(4-hydroxyphenyl)propan-2-one and 3-phenylbutan-2-one], some alipatic ketones (e.g. dodecan-2-one) and sulfides (e.g. 1-methyl-4-(methylsulfanyl)benzene).
References:
1. Malito, E., Alfieri, A., Fraaije, M.W. and Mattevi, A. Crystal structure of a Baeyer-Villiger monooxygenase. Proc. Natl. Acad. Sci. USA 101 (2004) 13157-13162. [PMID: 15328411]
2. Fraaije, M.W., Wu, J., Heuts, D.P., van Hellemond, E.W., Spelberg, J.H. and Janssen, D.B. Discovery of a thermostable Baeyer-Villiger monooxygenase by genome mining. Appl. Microbiol. Biotechnol. 66 (2005) 393-400. [PMID: 15599520]
Common name: nitrogenase
Reaction: 8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
For diagram click here.
Systematic name: reduced ferredoxin:dinitrogen oxidoreductase (ATP-hydrolysing)
Comments: Requires Mg2+. It is composed of two proteins that can be separated but are both required for nitrogenase activity. Dinitrogen reductase is a [4Fe-4S] protein, which, with two molecules of ATP and ferredoxin, generates an electron. The electron is transferred to the other protein, dinitrogenase (molybdoferredoxin). Dinitrogenase is a molybdenum-iron protein that reduces dinitrogen in three succesive two-electron reductions from nitrogen to diimine to hydrazine to two molecules of ammonia. The molybdenum may be replaced by vanadium or iron. The reduction is initiated by formation of hydrogen in stoichiometric amounts [2]. Acetylene is reduced to ethylene (but only very slowly to ethane), azide to nitrogen and ammonia, and cyanide to methane and ammonia. In the absence of a suitable substrate, hydrogen is slowly formed. Ferredoxin may be replaced by flavodoxin [see EC 1.19.6.1 nitrogenase (flavodoxin)]. Formerly EC 1.18.2.1.
Links to other databases: BRENDA, EXPASY, KEGG, UM-BBD, ERGO, PDB, CAS registry number: 9013-04-1
References:
1. Zumft, W.G., Paneque, A., Aparicio, P.J. and Losada, M. Mechanism of nitrate reduction in Chlorella. Biochem. Biophys. Res. Commun. 36 (1969) 980-986. [PMID: 4390523]
2. Liang, J. and Burris, R.H. Hydrogen burst associated with nitrogenase-catalyzed reactions. Proc. Natl. Acad. Sci. USA 85 (1988) 9446-9450. [PMID: 3200830]
3. Dance, I. The mechanism of nitrogenase. Computed details of the site and geometry of binding of alkyne and alkene substrates and intermediates. J. Am. Chem. Soc. 126 (2004) 11852-11863. [PMID: 15382920]
4. Chan, J.M., Wu, W., Dean, D.R. and Seefeldt, L.C. Construction and characterization of a heterodimeric iron protein: defining roles for adenosine triphosphate in nitrogenase catalysis. Biochemistry 39 (2000) 7221-7228. [PMID: 10852721]
Common name: aralkylamine N-acetyltransferase
Reaction: acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine
Other name(s): serotonin acetyltransferase; serotonin acetylase; arylalkylamine N-acetyltransferase; serotonin N-acetyltransferase; AANAT; melatonin rhythm enzyme
Systematic name: acetyl-CoA:2-arylethylamine N-acetyltransferase
Comments: Narrow specificity towards 2-arylethylamines, including serotonin (5-hydroxytryptamine), tryptamine, 5-methoxytryptamine and phenylethylamine. This is the penultimate enzyme in the production of melatonin (5-methoxy-N-acetyltryptamine) and controls its synthesis (cf. EC 2.1.1.4, acetylserotonin O-methyltransferase). Differs from EC 2.3.1.5 arylamine N-acetyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, PDB, CAS registry number: 92941-56-5
References:
1. Voisin, P., Namboodiri, M.A.A. and Klein, D.C. Arylamine N-acetyltransferase and arylalkylamine N-acetyltransferase in the mammalian pineal gland. J. Biol. Chem. 259 (1984) 10913-10918. [PMID: 6469990]
2. Ferry, G., Loynel, A., Kucharczyk, N., Bertin, S., Rodriguez, M., Delagrange, P., Galizzi, J.P., Jacoby, E., Volland, J.P., Lesieur, D., Renard, P., Canet, E., Fauchere, J.L. and Boutin, J.A. Substrate specificity and inhibition studies of human serotonin N-acetyltransferase. J. Biol. Chem. 275 (2000) 8794-8805. [PMID: 10722724]
3. Khalil, E.M. and Cole, P.A. A potent inhibitor of the melatonin rhythm enzyme. J. Am. Chem. Soc. 120 (1998) 6195-6196.
Common name: 3-oxoadipyl-CoA thiolase
Reaction: succinyl-CoA + acetyl-CoA = CoA + 3-oxoadipyl-CoA
For diagram click here.
Systematic name: succinyl-CoA:acetyl-CoA C-succinyltransferase
References:
1. Kaschabek, S.R., Kuhn, B., Müller, D., Schmidt, E. and Reineke, W. Degradation of aromatics and chloroaromatics by Pseudomonas sp. strain B13: purification and characterization of 3-oxoadipate:succinyl-coenzyme A (CoA) transferase and 3-oxoadipyl-CoA thiolase. J. Bacteriol. 184 (2002) 207-215. [PMID: 11741862]
2. Gobel, M., Kassel-Cati, K., Schmidt, E. and Reineke, W. Degradation of aromatics and chloroaromatics by Pseudomonas sp. strain B13: cloning, characterization, and analysis of sequences encoding 3-oxoadipate:succinyl-coenzyme A (CoA) transferase and 3-oxoadipyl-CoA thiolase. J. Bacteriol. 184 (2002) 216-223. [PMID: 11741863]
[EC 2.4.1.75 Deleted entry: insufficient evidence to conclude that this is a different enzyme from EC 2.4.1.43, polygalacturonate 4-α-galacturonosyltransferase (EC 2.4.1.75 created 1976, deleted 2005)]
Common name: NDP-glucose—starch glucosyltransferase
Reaction: NDP-glucose + (1,4-α-D-glucosyl)n = NDP + (1,4-α-D-glucosyl)n+1
Other name(s): granule-bound starch synthase; starch synthase II (ambiguous); waxy protein; starch granule-bound nucleoside diphosphate glucose-starch glucosyltransferase; granule-bound starch synthase I; GBSSI; granule-bound starch synthase II; GBSSII; GBSS; NDPglucose-starch glucosyltransferase
Systematic name: NDP-glucose:1,4-α-D-glucan 4-α-D-glucosyltransferase
Comments: Unlike EC 2.4.1.11, glycogen(starch) synthase and EC 2.4.1.21, starch synthase, which use UDP-glucose and ADP-glucose, respectively, this enzyme can use either UDP- or ADP-glucose. Mutants that lack the Wx (waxy) allele cannot produce this enzyme, which plays an important role in the normal synthesis of amylose. In such mutants, only amylopectin is produced in the endosperm [3] or pollen [5].
References:
1. Tsai, C.-Y. The function of the waxy locus in starch synthesis in maize endosperm. Biochem. Genet. 11 (1974) 83-96. [PMID: 4824506]
2. Nakamura, T., Vrinten, P., Hayakawa, K. and Ikeda, J. Characterization of a granule-bound starch synthase isoform found in the pericarp of wheat. Plant Physiol. 118 (1998) 451-459. [PMID: 9765530]
3. Fujita, N. and Taira, T. A 56-kDa protein is a novel granule-bound starch synthase existing in the pericarps, aleurone layers, and embryos of immature seed in diploid wheat (Triticum monococcum L.). Planta 207 (1998) 125-132. [PMID: 9951718]
4. Murai, J., Taira, T. and Ohta, D. Isolation and characterization of the three Waxy genes encoding the granule-bound starch synthase in hexaploid wheat. Gene 234 (1999) 71-79. [PMID: 10393240]
5. Nelson, O.E. The waxy locus in maize. II The location of the controlling element alleles. Genetics 60 (1968) 507-524.
Common name: phytoene synthase
Reaction: (1) 2 geranylgeranyl diphosphate = diphosphate + prephytoene diphosphate
(2) prephytoene diphosphate = phytoene + diphosphate
For diagram click here.
Other name(s): prephytoene-diphosphate synthase; phytoene synthetase; PSase; geranylgeranyl-diphosphate geranylgeranyltransferase
Systematic name: geranylgeranyl-diphosphate:geranylgeranyl-diphosphate geranylgeranyltransferase
Comments: Requires Mn2+ for activity. The enzyme appears to be stereospecific, normally producing 15-cis-phytoene. However, in Erwinia herbicola, the product is the 15-trans isomer [2].
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 57219-66-6 and 50936-61-3
References:
1. Gregonis, D.E. and Rilling, H.C. The stereochemistry of trans-phytoene synthesis. Some observations on lycopersene as a carotene precursor and a mechanism for the synthesis of cis- and trans-phytoene. Biochemistry 13 (1974) 1538-1542. [PMID: 4819767]
2. Iwata-Reuyl, D., Math, S.K., Desai, S.B. and Poulter, C.D. Bacterial phytoene synthase: molecular cloning, expression, and characterization of Erwinia herbicola phytoene synthase. Biochemistry 42 (2003) 3359-3365. [PMID: 12641468]
3. Misawa, N., Truesdale, M.R., Sandmann, G., Fraser, P.D., Bird, C., Schuch, W. and Bramley, P.M. Expression of a tomato cDNA coding for phytoene synthase in Escherichia coli, phytoene formation in vivo and in vitro, and functional analysis of the various truncated gene products. J. Biochem. (Tokyo) 116 (1994) 980-985. [PMID: 7896759]
Common name: aspartate—prephenate aminotransferase
Reaction: L-arogenate + oxaloacetate = prephenate + L-aspartate
For diagram click here.
Other name(s): prephenate transaminase (ambiguous); PAT (ambiguous); prephenate aspartate aminotransferase; L-aspartate:prephenate aminotransferase
Systematic name: L-arogenate:oxaloacetate aminotransferase
Comments: A pyridoxal-phosphate protein. Glutamate can also act as the amino donor, but more slowly (cf. EC 2.6.1.79, glutamate—prephenate aminotransferase).
References:
1. De-Eknamkul, W. and Ellis, B.E. Purification and characterization of prephenate aminotransferase from Anchusa officinalis cell cultures. Arch. Biochem. Biophys. 267 (1988) 87-94. [PMID: 3196038]
Common name: glutamate—prephenate aminotransferase
Reaction: L-arogenate + 2-oxoglutarate = prephenate + L-glutamate
For diagram click here.
Other name(s): prephenate transaminase (ambiguous); PAT (ambiguous); L-glutamate:prephenate aminotransferase
Systematic name: L-arogenate:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. Aspartate can also act as the amino donor, but more slowly (cf. EC 2.6.1.78, aspartate—prephenate aminotransferase). The enzyme from higher plants shows a marked preference for prephenate as substrate compared to pyruvate, phenylpyruvate or 4-hydroxyphenylpyruvate [1].
References:
1. Bonner, C.A. and Jensen, R.A. Novel features of prephenate aminotransferase from cell cultures of Nicotiana silvestris. Arch. Biochem. Biophys. 238 (1985) 237-246. [PMID: 3985619]
2. Siehl, D.L., Connelly, J.A. and Conn, E.E. Tyrosine biosynthesis in Sorghum bicolor: characteristics of prephenate aminotransferase. Z. Naturforsch. [C] 41 (1986) 79-86. [PMID: 2939644]
3. Bonner, C. and Jensen, R. Prephenate aminotransferase. Methods Enzymol. 142 (1987) 479-487. [PMID: 3298985]
Common name: nicotianamine aminotransferase
Reaction: nicotianamine + 2-oxoglutarate = 3"-deamino-3"-oxonicotianamine + L-glutamate
For diagram click here.
Other name(s): NAAT; NAAT-I; NAAT-II; NAAT-III
Systematic name: nicotianamine:2-oxoglutarate aminotransferase; nicotianamine transaminase
Comments: A pyridoxal-phosphate protein. This enzyme is produced by grasses. They secrete both the nicotianamine and the transaminated product into the soil around them. Both compounds chelate iron(II) and iron(III); these chelators, called mugineic acid family phytosiderophores, are taken up by the grass, which is thereby supplied with iron.
References:
1. Kanazawa, K., Higuchi, K., Nishizawa, N.-K., Fushiya, S., Chino, M. and Mori, S. Nicotianamine aminotransferase activities are correlated with the phytosiderophore secretions under Fe-deficient conditions in Gramineae. J. Exp. Bot. 45 (1994) 1903-1906.
2. Takahashi, M., Yamaguchi, H., Nakanishi, H., Shioiri, T., Nishizawa, N.K. and Mori, S. Cloning two genes for nicotianamine aminotransferase, a critical enzyme in iron acquisition (Strategy II) in graminaceous plants. Plant Physiol. 121 (1999) 947-956. [PMID: 10557244]
3. Schaaf, G., Ludewig, U., Erenoglu, B.E., Mori, S., Kitahara, T. and von Wirén, N. ZmYS1 functions as a proton-coupled symporter for phytosideorophore- and nicotianamine-chelated metals. J. Biol. Chem. 279 (2004) 9091-9096. [PMID: 14699112]
Common name: phosphoglucan, water dikinase
Reaction: ATP + [phospho-α-glucan] + H2O = AMP + O-phospho-[phospho-α-glucan] + phosphate
Other name(s): PWD; OK1
Systematic name: ATP:phospho-α-glucan, water phosphotransferase
Comments: The enzyme phosphorylates granular starch that has previously been phosphorylated by EC 2.7.9.4, α-glucan, water dikinase; there is no activity with unphosphorylated glucans. It transfers the β-phosphate of ATP to the phosphoglucan, whereas the γ-phosphate is transferred to water. In contrast to EC 2.7.9.4, which phosphorylates the glucose groups in glucans predominantly on O-6, this enzyme phosphorylates glucose groups in phosphorylated starch predominantly on O-3. The protein phosphorylates itself with the β-phosphate of ATP, which is then transferred to the glucan.
References:
1. Kötting, O., Pusch, K., Tiessen, A., Geigenberger, P., Steup, M. and Ritte, G. Identification of a novel enzyme required for starch metabolism in Arabidopsis leaves. The phosphoglucan, water dikinase. Plant Physiol. 137 (2005) 242-252. [PMID: 15618411]
Common name: scymnol sulfotransferase
Reaction: 3'-phosphoadenosine 5'-phosphosulfate + 5β-scymnol = adenosine 3',5'-bisphosphate + 5β-scymnol sulfate
For diagram click here.
Glossary and synonyms entries:
3'-phosphoadenosine 5'-phosphosulfate: a nucleotide sulfate
5β-scymnol sulfate = (24R,25S)-3α,7α,12α,24,27-pentahydroxy-5β-cholestan-26-yl sulfate
5α-cyprinol = 5α-cholestane-3α,7α,12α,26,27-pentol
Systematic name: 3'-phosphoadenosine 5'-phosphosulfate:5β-scymnol sulfotransferase
Comments: The enzyme from the shark Heterodontus portusjacksoni is able to sulfate the C27 bile salts 5β-scymnol (the natural bile salt) and 5α-cyprinol (the carp bile salt). Enzyme activity is activated by Mg2+ but inhibited by the product 5β-scymnol sulfate.
References:
1. Macrides, T.A., Faktor, D.A., Kalafatis, N. and Amiet, R.G. Enzymic sulfation of bile salts. Partial purification and characterization of an enzyme from the liver of the shark Heterodontus portusjacksoni that catalyses the sulfation of the shark bile steroid 5β-scymnol. Comp. Biochem. Physiol. Part B 107 (1994) 461-469. [PMID: 7749614]
2. Pettigrew, N.E., Wright, P.F.A. and Macrides, T.A. Investigation of 5β-scymnol sulfotransferase from the kidney and testes of Heterodontus portusjacksoni. Comp. Biochem. Physiol. Part B 121 (1998) 243-249.
3. Pettigrew, N.E., Wright, P.F.A. and Macrides, T.A. 5β-Scymnol sulfotransferase isolated from the tissues of an Australian shark species. Comp. Biochem. Physiol. Part B 121 (1998) 299-307.
4. Pettigrew, N.E., Wright, P.F.A. and Macrides, T.A. 5β-scymnol sulfotransferase isolated from the liver of two Australian ray species. Comp. Biochem. Physiol. Part B 121 (1998) 341-348.
Common name: oligosaccharide reducing-end xylanase
Reaction: Hydrolysis of 1,4-β-D-xylose residues from the reducing end of oligosaccharides
Other name(s): Rex; reducing end xylose-releasing exo-oligoxylanase
Systematic name: β-D-xylopyranosyl-(14)-β-D-xylopyranosyl-(14)-β-D-xylopyranose reducing-end xylanase
Comments: The enzyme acts rapidly on the β-anomer of β-D-xylopyranosyl-(14)-β-D-xylopyranosyl-(14)-β-D-xylopyranose, leaving the new reducing end in the α configuration. It also acts on longer oligosaccharides that have this structure at their reducing ends. The penultimate residue must be xylose, but replacing either of the other two residues with glucose merely slows the rate greatly.
References:
1. Honda, Y. and Kitaoka, M. A family 8 glycoside hydrolase from Bacillus halodurans C-125 (BH2105) is a reducing end xylose-releasing exo-oligoxylanase. J. Biol. Chem. 279 (2004) 55097-55103. [PMID: 15491996]
2. Fushinobu, S., Hidaka, M., Honda, Y., Wakagi, T., Shoun, H. and Kitaoka, M. Structural basis for the specificity of the reducing end xylose-releasing exo-oligoxylanase from Bacillus halodurans C-125. J. Biol. Chem. 2005 Feb 17 [Epub ahead of print] [PMID: 15718242]
Recommended name: mannan-binding lectin-associated serine protease-2
Reaction: Selective cleavage after Arg223 in complement component C2 (-Ser-Leu-Gly-Arg
Lys-Ile-Gln-Ile) and after Arg76 in complement component C4 (-Gly-Leu-Gln-ArgAla-Leu-Glu-Ile)
Other name(s): MASP-2; MBP-associated serine protease-2; mannose-binding lectin-associated serine protease-2; p100; mannan-binding lectin-associated serine peptidase
Comments: This enzyme displays C
-like esterolytic activity (cf. EC 3.4.21.42, complement subcomponent C) that specifically cleaves the complement proteins C2 and C4, thus activating the complement cascade. Belongs in peptidase family S1 (chymotrypsin family). The activity of the enzyme is modulated by mannan-binding lectin (MBL) [6].
References:
1. Matsushita, M. and Fujita, T. Activation of the classical complement pathway by mannose-binding protein in association with a novel C1s-like serine protease. J. Exp. Med. 176 (1992) 1497-1502. [PMID: 1460414]
2. Thiel, S., Vorup-Jensen, T., Stover, C.M., Schwaeble, W., Laursen, S.B., Poulsen, K., Willis, A.C., Eggleton, P., Hansen, S., Holmskov, U., Reid, K.B. and Jensenius, J.C. A second serine protease associated with mannan-binding lectin that activates complement. Nature 386 (1997) 506-510. [PMID: 9087411]
3. Rossi, V., Cseh, S., Bally, I., Thielens, N.M., Jensenius, J.C. and Arlaud, G.J. Substrate specificities of recombinant mannan-binding lectin-associated serine proteases-1 and -2. J Biol. Chem. 276 (2001) 40880-40887. [PMID: 11527969]
4. Ambrus, G., Gal, P., Kojima, M., Szilagyi, K., Balczer, J., Antal, J., Graf, L., Laich, A., Moffatt, B.E., Schwaeble, W., Sim, R.B. and Zavodszky, P. Natural substrates and inhibitors of mannan-binding lectin-associated serine protease-1 and -2: a study on recombinant catalytic fragments. J. Immunol. 170 (2003) 1374-1382. [PMID: 12538697]
5. Harmat, V., Gal, P., Kardos, J., Szilagyi, K., Ambrus, G., Vegh, B., Naray-Szabo, G. and Zavodszky, P. The structure of MBL-associated serine protease-2 reveals that identical substrate specificities of C1s and MASP-2 are realized through different sets of enzyme-substrate interactions. J. Mol. Biol. 342 (2004) 1533-1546. [PMID: 15364579]
6. Chen, C.B. and Wallis, R. Two mechanisms for mannose-binding protein modulation of the activity of its associated serine proteases. J. Biol. Chem. 279 (2004) 26058-26065. [PMID: 15060079]
Common name: N-substituted formamide deformylase
Reaction: N-benzylformamide + H2O = formate + benzylamine
For diagram click here.
Other name(s): NfdA
Systematic name: N-benzylformamide amidohydrolase
Comments: Zinc is a cofactor. While N-benzylformamide is the best substrate, the enzyme from Arthrobacter pascens can also act on the N-substituted formamides N-butylformamide, N-allylformamide, N-[2-(cyclohex-1-enyl)ethyl]formamide and N-(1-phenylethyl)formamide, but much more slowly. Amides of other acids do not act as substrates.
References:
1. Fukatsu, H., Hashimoto, Y., Goda, M., Higashibata, H. and Kobayashi, M. Amine-synthesizing enzyme N-substituted formamide deformylase: screening, purification, characterization, and gene cloning. Proc. Natl. Acad. Sci. USA 101 (2004) 13726-13731. [PMID: 15358859]
Common name: 4-hydroxyphenylacetate decarboxylase
Reaction: (4-hydroxyphenyl)acetate + H+ = 4-methylphenol + CO2
Other name(s): p-hydroxyphenylacetate decarboxylase; p-Hpd; 4-Hpd
Systematic name: 4-hydroxyphenylacetate carboxy-lyase
Comments: The enzyme, from the strict anaerobe Clostridium difficile, can also use (3,4-dihydroxyphenyl)acetate as a substrate, yielding 4-methylcatechol as a product. The enzyme is a glycyl radical enzyme.
References:
1. D'Ari, L., and Barker, H.A. p-Cresol formation by cell-free extracts of Clostridium difficile. Arch. Microbiol. 143 (1985) 311-312. [PMID: 3938267]
2. Selmer, T. and Andrei, P.I. p-Hydroxyphenylacetate decarboxylase from Clostridium difficile. A novel glycyl radical enzyme catalysing the formation of p-cresol. Eur. J. Biochem. 268 (2001) 1363-1372. [PMID: 11231288]
3. Andrei, P.I., Pierik, A.J., Zauner, S., Andrei-Selmer, L.C. and Selmer, T. Subunit composition of the glycyl radical enzyme p-hydroxyphenylacetate decarboxylase. A small subunit, HpdC, is essential for catalytic activity. Eur. J. Biochem. 271 (2004) 2225-2230. [PMID: 15153112]
Common name: arogenate dehydratase
Reaction: L-arogenate = L-phenylalanine + H2O + CO2
For diagram click here.
Other name(s): carboxycyclohexadienyl dehydratase
Systematic name: L-arogenate hydro-lyase (decarboxylating)
Comments: Also acts on prephenate and D-prephenyllactate. cf. EC 4.2.1.51, prephenate dehydratase.
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number:
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]