CATH Classification
Domain Context
CATH Clusters
Superfamily | MurE/MurF, N-terminal domain |
Functional Family | UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase |
Enzyme Information
6.3.2.10 |
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase.
based on mapping to UniProt P11880
ATP + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysine + D-alanyl- D-alanine = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D- glutamyl-L-lysyl-D-alanyl-D-alanine.
-!- Involved with EC 6.3.2.4, EC 6.3.2.7 or EC 6.3.2.13, EC 6.3.2.8 and EC 6.3.2.9 in the synthesis of a cell-wall peptide. -!- Also catalyzes the reaction when the C-terminal residue of the tripeptide is meso-2,4-diaminoheptanedioate (acylated at its L-center), linking the D-Ala--D-Ala to the carboxy group of the L-center. -!- Formerly EC 6.3.2.15.
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UniProtKB Entries (1)
P11880 |
MURF_ECOLI
Escherichia coli K-12
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
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PDB Structure
PDB | 1GG4 |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | Escherichia |
Primary Citation |
Crystal structure of Escherichia coli UDPMurNAc-tripeptide d-alanyl-d-alanine-adding enzyme (MurF) at 2.3 A resolution.
J.Mol.Biol.
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