IUBMB Enzyme Nomenclature

EC 6.2.1.54

Accepted name: D-alanine—[D-alanyl-carrier protein] ligase

Reaction: ATP + D-alanine + holo-[D-alanyl-carrier protein] = AMP + diphosphate + D-alanyl-[D-alanyl-carrier protein] (overall reaction)
(1a) ATP + D-alanine = (D-alanyl)adenylate + diphosphate
(1b) (D-alanyl)adenylate + holo-[D-alanyl-carrier protein] = AMP + D-alanyl-[D-alanyl-carrier protein]

Other name(s): dltA (gene name); Dcl

Systematic name: D-alanine:[D-alanyl-carrier protein] ligase

Comments: The enzyme is involved in the modification of wall teichoic acids, as well as type I and IV lipoteichoic acids, with D-alanine residues. It activates D-alanine using ATP to form a high-energy (D-alanyl)adenylate intermediate and subsequently transfers the alanyl moiety to the phosphopantheinyl prosthetic group of a D-alanyl-carrier protein (DltC).

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:

References:

1. Perego, M., Glaser, P., Minutello, A., Strauch, M.A., Leopold, K. and Fischer, W. Incorporation of D-alanine into lipoteichoic acid and wall teichoic acid in Bacillus subtilis. Identification of genes and regulation. J. Biol. Chem. 270 (1995) 15598-15606. [PMID: 7797557]

2. Yonus, H., Neumann, P., Zimmermann, S., May, J.J., Marahiel, M.A. and Stubbs, M.T. Crystal structure of DltA. Implications for the reaction mechanism of non-ribosomal peptide synthetase adenylation domains. J. Biol. Chem. 283 (2008) 32484-32491. [PMID: 18784082]

3. Du, L., He, Y. and Luo, Y. Crystal structure and enantiomer selection by D-alanyl carrier protein ligase DltA from Bacillus cereus. Biochemistry 47 (2008) 11473-11480. [PMID: 18847223]

4. Osman, K.T., Du, L., He, Y. and Luo, Y. Crystal structure of Bacillus cereus D-alanyl carrier protein ligase (DltA) in complex with ATP. J. Mol. Biol. 388 (2009) 345-355. [PMID: 19324056]

[EC 6.2.1.54 created 2018]


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