Enzymes
UniProtKB help_outline | 1,464 proteins |
Enzyme class help_outline |
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GO Molecular Function help_outline |
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Reaction participants Show >> << Hide
- Name help_outline di-trans,octa-cis-undecaprenyl phosphate Identifier CHEBI:60392 Charge -2 Formula C55H89O4P InChIKeyhelp_outline UFPHFKCTOZIAFY-NTDVEAECSA-L SMILEShelp_outline CC(C)=CCC\C(C)=C\CC\C(C)=C\CC\C(C)=C/CC\C(C)=C/CC\C(C)=C/CC\C(C)=C/CC\C(C)=C/CC\C(C)=C/CC\C(C)=C/CC\C(C)=C/COP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 15 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline UDP-N-acetyl-α-D-muramoyl-L-alanyl-γ-D-glutamyl-L-lysyl-D-alanyl-D-alanine Identifier CHEBI:70758 Charge -3 Formula C40H62N9O26P2 InChIKeyhelp_outline PFMVORMCVGOQKR-XNCOKRRHSA-K SMILEShelp_outline C[C@@H](NC(=O)[C@@H](C)NC(=O)[C@H](CCCC[NH3+])NC(=O)CC[C@@H](NC(=O)[C@H](C)NC(=O)[C@@H](C)O[C@H]1[C@H](O)[C@@H](CO)O[C@H](OP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2ccc(=O)[nH]c2=O)[C@@H]1NC(C)=O)C([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate Identifier CHEBI:60032 Charge -3 Formula C86H140N7O21P2 InChIKeyhelp_outline SULOOAFLXMQJSF-OGDYFQGPSA-K SMILEShelp_outline C[C@@H](NC(=O)[C@@H](C)NC(=O)[C@H](CCCC[NH3+])NC(=O)CC[C@@H](NC(=O)[C@H](C)NC(=O)[C@@H](C)O[C@H]1[C@H](O)[C@@H](CO)O[C@H](OP([O-])(=O)OP([O-])(=O)OC\C=C(\C)CC\C=C(\C)CC\C=C(\C)CC\C=C(\C)CC\C=C(\C)CC\C=C(\C)CC\C=C(\C)CC\C=C(\C)CC\C=C(/C)CC\C=C(/C)CCC=C(C)C)[C@@H]1NC(C)=O)C([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline UMP Identifier CHEBI:57865 (Beilstein: 3570858) help_outline Charge -2 Formula C9H11N2O9P InChIKeyhelp_outline DJJCXFVJDGTHFX-XVFCMESISA-L SMILEShelp_outline O[C@@H]1[C@@H](COP([O-])([O-])=O)O[C@H]([C@@H]1O)n1ccc(=O)[nH]c1=O 2D coordinates Mol file for the small molecule Search links Involved in 53 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:21920 | RHEA:21921 | RHEA:21922 | RHEA:21923 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Purification and characterization of the bacterial MraY translocase catalyzing the first membrane step of peptidoglycan biosynthesis.
Bouhss A., Crouvoisier M., Blanot D., Mengin-Lecreulx D.
The MraY translocase catalyzes the first membrane step of bacterial cell wall peptidoglycan synthesis (i.e. the transfer of the phospho-N-acetylmuramoyl-pentapeptide motif onto the undecaprenyl phosphate carrier lipid), a reversible reaction yielding undecaprenylpyrophosphoryl-N-acetylmuramoyl-pen ... >> More
The MraY translocase catalyzes the first membrane step of bacterial cell wall peptidoglycan synthesis (i.e. the transfer of the phospho-N-acetylmuramoyl-pentapeptide motif onto the undecaprenyl phosphate carrier lipid), a reversible reaction yielding undecaprenylpyrophosphoryl-N-acetylmuramoyl-pentapeptide (lipid intermediate I). This essential integral membrane protein, which is considered as a very promising target for the search of new antibacterial compounds, has thus far been clearly underexploited due to its intrinsic refractory nature to overexpression and purification. We here report conditions for the high level overproduction and for the first time the purification to homogeneity of milligram quantities of MraY protein. The kinetic parameters and effects of pH, salts, cations, and detergents on enzyme activity are described, taking the Bacillus subtilis MraY translocase as a model. << Less
J Biol Chem 279:29974-29980(2004) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Recent advances in the formation of the bacterial peptidoglycan monomer unit.
van Heijenoort J.
Nat Prod Rep 18:503-519(2001) [PubMed] [EuropePMC]
This publication is cited by 11 other entries.
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On the initial stage in peptidoglycan synthesis. Phospho-N-acetylmuramyl-pentapeptide translocase (uridine monophosphate).
Struve W.G., Sinha R.K., Neuhaus F.C.
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The initial stage in peptidoglycan synthesis. IV. Solubilization of phospho-N-acetylmuramyl-pentapeptide translocase.
Heydanek M.G. Jr., Neuhaus F.C.
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Structure of a lipid intermediate in cell wall peptidoglycan synthesis: a derivative of a C55 isoprenoid alcohol.
Higashi Y., Strominger J.L., Sweeley C.C.
Proc Natl Acad Sci U S A 57:1878-1884(1967) [PubMed] [EuropePMC]