The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

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 covalently-bound phosphopantheinyl cofactor of a D-alanyl-carrier protein (DltC).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 19324056]
[EC 6.2.1.54 created 2018]
 
 


Data © 2001–2024 IUBMB
Web site © 2005–2024 Andrew McDonald