Enzymes
| UniProtKB help_outline | 1 proteins |
Reaction participants Show >> << Hide
- Name help_outline benzylamine Identifier CHEBI:225238 (Beilstein: 12297043) help_outline Charge 1 Formula C7H10N InChIKeyhelp_outline WGQKYBSKWIADBV-UHFFFAOYSA-O SMILEShelp_outline [NH3+]Cc1ccccc1 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline pyruvate Identifier CHEBI:15361 (Beilstein: 3587721; CAS: 57-60-3) help_outline Charge -1 Formula C3H3O3 InChIKeyhelp_outline LCTONWCANYUPML-UHFFFAOYSA-M SMILEShelp_outline CC(=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 213 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline benzaldehyde Identifier CHEBI:17169 (CAS: 100-52-7) help_outline Charge 0 Formula C7H6O InChIKeyhelp_outline HUMNYLRZRPPJDN-UHFFFAOYSA-N SMILEShelp_outline O=Cc1ccccc1 2D coordinates Mol file for the small molecule Search links Involved in 14 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-alanine Identifier CHEBI:57972 Charge 0 Formula C3H7NO2 InChIKeyhelp_outline QNAYBMKLOCPYGJ-REOHCLBHSA-N SMILEShelp_outline C[C@H]([NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 107 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:64272 | RHEA:64273 | RHEA:64274 | RHEA:64275 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Identification of omega-aminotransferase from Caulobacter crescentus and site-directed mutagenesis to broaden substrate specificity.
Hwang B.Y., Ko S.H., Park H.Y., Seo J.H., Lee B.S., Kim B.G.
A putative aminotransferase gene, cc3143 (aptA), from Caulobacter crescentus was screened by bioinformatical tools and overexpressed in E. coli, and the substrate specificity of the aminotransferase was investigated. AptA showed high activity for short-chain beta-amino acids. It showed the highest ... >> More
A putative aminotransferase gene, cc3143 (aptA), from Caulobacter crescentus was screened by bioinformatical tools and overexpressed in E. coli, and the substrate specificity of the aminotransferase was investigated. AptA showed high activity for short-chain beta-amino acids. It showed the highest activity for 3-amino-n-butyric acid. It showed higher activity toward aromatic amines than aliphatic amines. The 3D model of the aminotransferase was constructed by homology modeling using a dialkylglycine decarboxylase PDB ID: 1DGE) as a template. Then, the aminotransferase was rationally redesigned to increase the activity for 3-amino-3-phenylpropionic acid. The mutants N285A and V227G increased the relative activity for 3-amino-3-phenylpropionic acid to 3-amino-n-butyric acid by 11-fold and 3-fold, respectively, over that of wild type. << Less
J. Microbiol. Biotechnol. 18:48-54(2008) [PubMed] [EuropePMC]
This publication is cited by 6 other entries.