SSF53623

MurD-like peptide ligases, catalytic domain

SUPERFAMILY entry
Member databaseSUPERFAMILY
SUPERFAMILY typehomologous superfamily

Description
Imported from IPR036565

Mur ligases play an essential role in the intracellular biosynthesis of bacterial peptidoglycan. Mur ligases share the same three-domain topology, with N-terminal and central domains responsible for binding the UDP-precursor and ATP, respectively, while the C-terminal part binds the condensing amino acid residue
[2, 3]
.

This superfamily represents the central domain from all four Mur enzymes: UDP-N-acetylmuramate-L-alanine ligase (MurC), UDP-N-acetylmuramoylalanine-D-glutamate ligase (MurD), UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase (MurE), and UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase (MurF). It also includes folylpolyglutamate synthase that transfers glutamate to folylpolyglutamate and cyanophycin synthetase that catalyses the biosynthesis of the cyanobacterial reserve material multi-L-arginyl-poly-L-aspartate (cyanophycin)
[1]
.

References
Imported from IPR036565

1.Molecular characterization of cyanophycin synthetase, the enzyme catalyzing the biosynthesis of the cyanobacterial reserve material multi-L-arginyl-poly-L-aspartate (cyanophycin). Ziegler K, Diener A, Herpin C, Richter R, Deutzmann R, Lockau W. Eur. J. Biochem. 254, 154-9, (1998). View articlePMID: 9652408

2.Structural and functional characterization of enantiomeric glutamic acid derivatives as potential transition state analogue inhibitors of MurD ligase. Kotnik M, Humljan J, Contreras-Martel C, Oblak M, Kristan K, Herve M, Blanot D, Urleb U, Gobec S, Dessen A, Solmajer T. J. Mol. Biol. 370, 107-15, (2007). View articlePMID: 17507028

3.Crystallographic Study of Peptidoglycan Biosynthesis Enzyme MurD: Domain Movement Revisited. Sink R, Kotnik M, Zega A, Barreteau H, Gobec S, Blanot D, Dessen A, Contreras-Martel C. PLoS One 11, e0152075, (2016). PMID: 27031227

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