Enzymes
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- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; 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 6,204 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline N-(long-chain-fatty-acyl)-L-glutamate Identifier CHEBI:17583 Charge -2 Formula C6H6NO5R SMILEShelp_outline [O-]C(=O)CC[C@H](NC([*])=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
- Name help_outline a long-chain fatty acid Identifier CHEBI:57560 Charge -1 Formula CO2R SMILEShelp_outline [O-]C([*])=O 2D coordinates Mol file for the small molecule Search links Involved in 727 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-glutamate Identifier CHEBI:29985 (CAS: 11070-68-1) help_outline Charge -1 Formula C5H8NO4 InChIKeyhelp_outline WHUUTDBJXJRKMK-VKHMYHEASA-M SMILEShelp_outline [NH3+][C@@H](CCC([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 244 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:17517 | RHEA:17518 | RHEA:17519 | RHEA:17520 | |
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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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A new enzyme: long acyl aminoacylase from Pseudomonas diminuta.
Fukuda H., Iwade S., Kimura A.
A new enzyme which hydrolyzes N-long chain acyl glutamic acid was found in cell-free extracts of Pseudomonas diminuta. Two active fractions (long acyl aminoacylase I and II) were separated by DEAE-cellulose column chromatography. The long acyl aminoacylase I was purified about 650-fold, and the pu ... >> More
A new enzyme which hydrolyzes N-long chain acyl glutamic acid was found in cell-free extracts of Pseudomonas diminuta. Two active fractions (long acyl aminoacylase I and II) were separated by DEAE-cellulose column chromatography. The long acyl aminoacylase I was purified about 650-fold, and the purified preparation was electrophoretically homogeneous. The molecular weight was estimated to be 300,000 by gel filtration. The enzyme was unique in its substrate specificity. It hydrolyzed only N-long acyl glutamic acid and could not react with other N-acyl amino acids. Lauroyl (C12)-, myristoyl (C14)-, and palmitoyl (C16)-glutamic acid were good substrates, but acetyl glutamic acid was not hydrolyzed. Therefore this enzyme is considered to be a new acylase which is specific for N-long chain acyl glutamic acid, and it is designated as N-long acyl glutamic acid amidohydrolase [EC 3.5.1 group]. << Less