Mur ligase
From Proteopedia
(Difference between revisions)
| Line 2: | Line 2: | ||
'''MurD ligase''' or '''UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase''' catalyzes the conversion of UDP-N-acetylmuramoyl-L-alanine (UMA), D-glutamate and ATP to UDP-N-acetylmuramoyl-L-alanine-D-glutamate and ADP. MurD is one of four Mur ubiquitin ligase enzymes (MurC, MurD, MurE, MurF) which participate in the biosynthesis of peptidoglycans. All four enzymes are topologically similar and contain N-terminal domain which binds the substrate, an ATP-binding central domain and a C-terminal domain which binds the incorporated amino acid. | '''MurD ligase''' or '''UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase''' catalyzes the conversion of UDP-N-acetylmuramoyl-L-alanine (UMA), D-glutamate and ATP to UDP-N-acetylmuramoyl-L-alanine-D-glutamate and ADP. MurD is one of four Mur ubiquitin ligase enzymes (MurC, MurD, MurE, MurF) which participate in the biosynthesis of peptidoglycans. All four enzymes are topologically similar and contain N-terminal domain which binds the substrate, an ATP-binding central domain and a C-terminal domain which binds the incorporated amino acid. | ||
| + | </StructureSection> | ||
== 3D Structures of MurD ligase == | == 3D Structures of MurD ligase == | ||
Revision as of 10:01, 1 December 2014
| |||||||||||
3D Structures of MurD ligase
Updated on 01-December-2014
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Jaime Prilusky, Joel L. Sussman
