Enzymes
| UniProtKB help_outline | 1 proteins |
| Enzyme class help_outline |
|
Reaction participants Show >> << Hide
- Name help_outline L-canavanine Identifier CHEBI:78902 Charge 1 Formula C5H13N4O3 InChIKeyhelp_outline FSBIGDSBMBYOPN-VKHMYHEASA-O SMILEShelp_outline NC(=[NH2+])NOCC[C@H]([NH3+])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 L-ornithine Identifier CHEBI:46911 Charge 1 Formula C5H13N2O2 InChIKeyhelp_outline AHLPHDHHMVZTML-BYPYZUCNSA-O SMILEShelp_outline [NH3+]CCC[C@H]([NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 50 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-arginine Identifier CHEBI:32682 Charge 1 Formula C6H15N4O2 InChIKeyhelp_outline ODKSFYDXXFIFQN-BYPYZUCNSA-O SMILEShelp_outline NC(=[NH2+])NCCC[C@H]([NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 72 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-canaline Identifier CHEBI:145769 Charge 0 Formula C4H10N2O3 InChIKeyhelp_outline FQPGMQABJNQLLF-VKHMYHEASA-N SMILEShelp_outline C(C[C@@H](C([O-])=O)[NH3+])ON 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
Cross-references
| RHEA:62444 | RHEA:62445 | RHEA:62446 | RHEA:62447 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
|
|||
| EC numbers help_outline |
Publications
-
Characterization of AmtA, an amidinotransferase involved in the biosynthesis of phaseolotoxins.
Li M., Chen L., Deng Z., Zhao C.
Phaseolotoxins (PHTs), which are produced by Pseudomonas, belong to a family of phosphoramidate natural products. Two nonproteinogenic amino acid precursors, N(δ)(N'-sulfo-diaminophosphinyl)-ornithine (PSOrn) and homoarginine (hArg), are involved in biosynthesis of PHTs. Amidinotransferase AmtA ca ... >> More
Phaseolotoxins (PHTs), which are produced by Pseudomonas, belong to a family of phosphoramidate natural products. Two nonproteinogenic amino acid precursors, N(δ)(N'-sulfo-diaminophosphinyl)-ornithine (PSOrn) and homoarginine (hArg), are involved in biosynthesis of PHTs. Amidinotransferase AmtA catalyses the formation of hArg, with arginine and lysine as substrates. AmtA was overexpressed and purified in an Escherichia coli system. An in vitro enzyme assay showed that it has stricter substrate specificity than certain other amidinotransferases. Site-directed mutagenesis experiments showed that the mutation AmtA Met243His244 is an alternative while Met246 is essential for the transamidination activity. << Less
FEBS Open Bio 6:603-609(2016) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.