Enzymes
| UniProtKB help_outline | 2 proteins |
| Enzyme class help_outline |
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Name help_outline
N-(6-aminohexanoyl)-6-aminohexanoic acid zwitterion
Identifier
CHEBI:78629
Charge
0
Formula
(C6H11NO)n.C6H13NO2
Search links
Involved in 1 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
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Identifier: RHEA-COMP:9820Polymer name: [N-(6-aminohexanoyl)](n)Polymerization index help_outline nFormula C6H13NO2(C6H11NO)nCharge (0)(0)nMol File for the polymer
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Identifier: RHEA-COMP:14302Polymer name: [N-(6-aminohexanoyl)](n-1)Polymerization index help_outline n-1Formula C6H13NO2(C6H11NO)n-1Charge (0)(0)n-1Mol File for the polymer
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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 6,048 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 6-aminohexanoate Identifier CHEBI:57826 Charge 0 Formula C6H13NO2 InChIKeyhelp_outline SLXKOJJOQWFEFD-UHFFFAOYSA-N SMILEShelp_outline [NH3+]CCCCCC([O-])=O 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
Cross-references
| RHEA:18225 | RHEA:18226 | RHEA:18227 | RHEA:18228 | |
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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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Purification and characterization of 6-aminohexanoic-acid-oligomer hydrolase of Flavobacterium sp. Ki72.
Kinoshita S., Terada T., Taniguchi T., Takene Y., Masuda S., Matsunaga N., Okada H.
6-Aminohexanoic-oligomer hydrolase of Flavobacterium sp. KI72 was purified to homogeneity by column chromatography three times, and by preparation polyacrylamide gel electrophoresis twice. The purified enzyme had the following characteristics. 1. The molecular weight was estimated to be 84000 by S ... >> More
6-Aminohexanoic-oligomer hydrolase of Flavobacterium sp. KI72 was purified to homogeneity by column chromatography three times, and by preparation polyacrylamide gel electrophoresis twice. The purified enzyme had the following characteristics. 1. The molecular weight was estimated to be 84000 by Sephadex G-200 molecular-sieve chromatography. The enzyme consisted of two homologous subunits of 42000, judged from sodium dodecylsulfate/polyacrylamide gel electrophoresis. 2. The optimum pH for activity was between 8 and 9, the optimum temperature was 40 degrees C for a 1-h reaction. The Michaelis-Menten constants and turnover numbers for the 6-aminohexanoic acid dimer and trimer were 5.9 mM and 2.4 s-1, and 6.2 mM and 2.0 s-1 respectively. 3. The enzyme was inhibited by 0.37 mM diisopropylfluorophosphate and by 0.013 mM p-chloromercuribenzoate. 4. The enzyme was active on 6-aminohexanoic acid oligomers from dimer to hexamer and icosamer but not on hectamer, and the activity decreased with the increase of the polymerization number of the oligomer. The oligomers were hydrolyzed so as to remove the 6-aminohexanoic acid residue successively from the amino terminus. The enzyme could not hydrolyze other linear amides, cyclic amides, dipeptides, tripeptides or casein. 5. 6-aminohexanoic-acid-oligomer hydrolase was classified as a new member of the linear amidases (EC 3.5.1.-). << Less
Eur J Biochem 116:547-551(1981) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.