Enzymes
| UniProtKB help_outline | 1,583 proteins |
| Enzyme class help_outline |
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Reaction participants Show >> << Hide
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Namehelp_outline
Nπ-phospho-L-histidyl-[protein]
Identifier
RHEA-COMP:9746
Reactive part
help_outline
- Name help_outline Nπ-phospho-L-histidine residue Identifier CHEBI:64837 Charge -2 Formula C6H6N3O4P SMILEShelp_outline C(*)(=O)[C@@H](N*)CC=1N(C=NC1)P([O-])(=O)[O-] 2D coordinates Mol file for the small molecule Search links Involved in 24 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline N-acetyl-β-D-muramate Identifier CHEBI:64848 Charge -1 Formula C11H18NO8 InChIKeyhelp_outline MNLRQHMNZILYPY-YVNCZSHWSA-M SMILEShelp_outline C[C@@H](O[C@H]1[C@H](O)[C@@H](CO)O[C@@H](O)[C@@H]1NC(C)=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
L-histidyl-[protein]
Identifier
RHEA-COMP:9745
Reactive part
help_outline
- Name help_outline L-histidine residue Identifier CHEBI:29979 Charge 0 Formula C6H7N3O SMILEShelp_outline C(*)(=O)[C@@H](N*)CC=1N=CNC1 2D coordinates Mol file for the small molecule Search links Involved in 40 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline N-acetyl-β-D-muramate 6-phosphate Identifier CHEBI:58721 Charge -3 Formula C11H17NO11P InChIKeyhelp_outline NMEMTQKUEVNSPV-YVNCZSHWSA-K SMILEShelp_outline C[C@@H](O[C@H]1[C@H](O)[C@@H](COP([O-])([O-])=O)O[C@@H](O)[C@@H]1NC(C)=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
Cross-references
| RHEA:33399 | RHEA:33400 | RHEA:33401 | RHEA:33402 | |
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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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Identification of a phosphotransferase system of Escherichia coli required for growth on N-acetylmuramic acid.
Dahl U., Jaeger T., Nguyen B.T., Sattler J.M., Mayer C.
We report here that wild-type Escherichia coli grows on N-acetylmuramic acid (MurNAc) as the sole source of carbon and energy. Analysis of mutants defective in N-acetylglucosamine (GlcNAc) catabolism revealed that the catabolic pathway for MurNAc merges into the GlcNAc pathway on the level of GlcN ... >> More
We report here that wild-type Escherichia coli grows on N-acetylmuramic acid (MurNAc) as the sole source of carbon and energy. Analysis of mutants defective in N-acetylglucosamine (GlcNAc) catabolism revealed that the catabolic pathway for MurNAc merges into the GlcNAc pathway on the level of GlcNAc 6-phosphate. Furthermore, analysis of mutants defective in components of the phosphotransferase system (PTS) revealed that a PTS is essential for growth on MurNAc. However, neither the glucose-, mannose/glucosamine-, nor GlcNAc-specific PTS (PtsG, ManXYZ, and NagE, respectively) was found to be necessary. Instead, we identified a gene at 55 min on the E. coli chromosome that is responsible for MurNAc uptake and growth. It encodes a single polypeptide consisting of the EIIB and C domains of a so-far-uncharacterized PTS that was named murP. MurP lacks an EIIA domain and was found to require the activity of the crr-encoded enzyme IIA-glucose (EIIA(Glc)), a component of the major glucose transport system for growth on MurNAc. murP deletion mutants were unable to grow on MurNAc as the sole source of carbon; however, growth was rescued by providing murP in trans expressed from an isopropylthiogalactopyranoside-inducible plasmid. A functional His(6) fusion of MurP was constructed, isolated from membranes, and identified as a polypeptide with an apparent molecular mass of 37 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blot analysis. Close homologs of MurP were identified in the genome of several bacteria, and we believe that these organisms might also be able to utilize MurNAc. << Less