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- Name help_outline N-benzoylglycine Identifier CHEBI:606565 Charge -1 Formula C9H8NO3 InChIKeyhelp_outline QIAFMBKCNZACKA-UHFFFAOYSA-M SMILEShelp_outline [O-]C(=O)CNC(=O)c1ccccc1 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 H2O Identifier CHEBI:15377 (CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,337 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline benzoate Identifier CHEBI:16150 (CAS: 766-76-7) help_outline Charge -1 Formula C7H5O2 InChIKeyhelp_outline WPYMKLBDIGXBTP-UHFFFAOYSA-M SMILEShelp_outline [O-]C(=O)c1ccccc1 2D coordinates Mol file for the small molecule Search links Involved in 17 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline glycine Identifier CHEBI:57305 Charge 0 Formula C2H5NO2 InChIKeyhelp_outline DHMQDGOQFOQNFH-UHFFFAOYSA-N SMILEShelp_outline [NH3+]CC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 151 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:10424 | RHEA:10425 | RHEA:10426 | RHEA:10427 | |
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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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Enzymatic activity of Campylobacter jejuni hippurate hydrolase.
Steele M., Marcone M., Gyles C., Chan V.L., Odumeru J.
The hippurate hydrolase enzyme of Campylobacter jejuni was expressed in Escherichia coli as a six-histidine-tagged fusion protein. The purified recombinant enzyme was characterized to gain an understanding of the structure and activity of the hippurate hydrolase. The recombinant enzyme had a nativ ... >> More
The hippurate hydrolase enzyme of Campylobacter jejuni was expressed in Escherichia coli as a six-histidine-tagged fusion protein. The purified recombinant enzyme was characterized to gain an understanding of the structure and activity of the hippurate hydrolase. The recombinant enzyme had a native molecular mass of 193+/- 11 kDa a reduced molecular mass of 42.4+/-0.8 kDa, and possessed 1.98+/-0.68 molecules of zinc per enzyme subunit molecule, suggesting that it was a homotetramer with two associated zinc ions. The enzyme was a metallocarboxypeptidase that was sensitive to silver, copper and ferrous ions, and displayed optimal activity at pH 7.5 and 50 degrees C. It hydrolyzed carboxypeptidase substrates in vitro, displaying its highest activity against N-benzoyl-linked small aliphatic amino acids. A high proportion of the enzyme structure consisted of highly ordered alpha-helix and beta-sheet sequences. An alignment of the amino acid sequence of the hippurate hydrolase enzyme with those of related enzymes with similar activities revealed several conserved amino acids, which might be involved in enzyme catalysis or metal ion binding for the enzyme. Site-directed mutagenesis of the recombinant enzyme demonstrated that the Asp(76), Aps(104), Glu(134), Glu(135), His(161) and His(356) positions were important for the catalytic activity of the enzyme. << Less