EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
6.3.2.13 | ATP + UDP-MurNAc-L-Ala-D-Glu + L-cystathionine |
relative activity wild-type: 12% |
Mycobacterium tuberculosis |
? |
- |
? |
6.3.2.13 | ATP + UDP-MurNAc-L-Ala-D-Glu + L-Lys |
relative activity wild-type: 7% |
Mycobacterium tuberculosis |
? |
- |
? |
6.3.2.13 | ATP + UDP-MurNAc-L-Ala-D-Glu + meso-2,6-diaminoheptanedioate |
- |
Bacillus subtilis |
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diaminoheptanedioate |
- |
? |
6.3.2.13 | ATP + UDP-MurNAc-L-Ala-D-Glu + meso-2,6-diaminoheptanedioate |
- |
Escherichia coli |
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diaminoheptanedioate |
- |
? |
6.3.2.13 | ATP + UDP-MurNAc-L-Ala-D-Glu + meso-2,6-diaminoheptanedioate |
- |
Lysinibacillus sphaericus |
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diaminoheptanedioate |
- |
? |
6.3.2.13 | ATP + UDP-MurNAc-L-Ala-D-Glu + meso-2,6-diaminoheptanedioate |
r |
Escherichia coli |
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diaminoheptanedioate |
- |
? |
6.3.2.13 | ATP + UDP-MurNAc-L-Ala-D-Glu + meso-2,6-diaminoheptanedioate |
r |
Bacillus cereus |
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diaminoheptanedioate |
- |
? |
6.3.2.13 | ATP + UDP-MurNAc-L-Ala-D-Glu + meso-2,6-diaminoheptanedioate |
specific for UDP-N-MurNAc-L-Ala-D-Glu and meso-2,6-diaminoheptanedioate |
Bacillus cereus |
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diaminoheptanedioate |
- |
? |
6.3.2.13 | ATP + UDP-MurNAc-L-Ala-D-Glu + meso-2,6-diaminoheptanedioate |
relative activity wild-type: 100% |
Mycobacterium tuberculosis |
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diaminoheptanedioate |
- |
? |
6.3.2.13 | ATP + UDP-MurNAc-L-Ala-D-Glu + meso-2,6-diaminoheptanedioate |
the threedimensional structure of MurE from Mycobacterium leprae is modeled using comparative modeling methods based on the X-ray crystal structure of MurE from Escherichia coli. The docked complexes reveal the amino acids responsible for binding the substrates. Superposition of these complex structures suggests that carboxylic acid group of UDP-Nacetyl muramoyl-glycyl-D-glutamate is positioned in proximity to gamma-phosphate of the ATP to facilitate the formation of acylphosphate intermediate. The orientation of an amino group of meso-diaminopimelic acid facilitates the nucleophilic attack to form the product |
Mycobacterium leprae |
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diaminoheptanedioate |
- |
? |