Member database | Pfam |
Pfam type | family |
Short name | Dala_Dala_lig_C |
Clan | ATP-grasp |
Author | Bateman A;0000-0002-6982-4660 Moxon SJ;0000-0003-4644-1816 |
Sequence Ontology | 0100021 |
Description
This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF)
[1].
References
1.Roles of Mycobacterium smegmatis D-alanine:D-alanine ligase and D-alanine racemase in the mechanisms of action of and resistance to the peptidoglycan inhibitor D-cycloserine. Feng Z, Barletta RG. Antimicrob. Agents Chemother. 47, 283-91, (2003). View articlePMID: 12499203
Further reading
2. D-alanine:D-alanine ligase: phosphonate and phosphinate intermediates with wild type and the Y216F mutant. Fan C, Park IS, Walsh CT, Knox JR. Biochemistry 36, 2531-8, (1997). View articlePMID: 9054558
3. The molecular basis of vancomycin resistance in clinically relevant Enterococci: crystal structure of D-alanyl-D-lactate ligase (VanA). Roper DI, Huyton T, Vagin A, Dodson G. Proc. Natl. Acad. Sci. U.S.A. 97, 8921-5, (2000). View articlePMID: 10908650
Integrated to
Representative structure
1iow: COMPLEX OF Y216F D-ALA:D-ALA LIGASE WITH ADP AND A PHOSPHORYL PHOSPHINATE