Enzymes
| UniProtKB help_outline | 4 proteins |
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- Name help_outline an amide Identifier CHEBI:140324 Charge 0 Formula CH2NOR SMILEShelp_outline N(C(*)=O)([H])[H] 2D coordinates Mol file for the small molecule Search links Involved in 43 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a nitrile Identifier CHEBI:18379 Charge 0 Formula CNR SMILEShelp_outline [*]C#N 2D coordinates Mol file for the small molecule Search links Involved in 113 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 6,648 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:85699 | RHEA:85700 | RHEA:85701 | RHEA:85702 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Related reactions help_outline
Specific form(s) of this reaction
Publications
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Characterization of a new cobalt-containing nitrile hydratase purified from urea-induced cells of Rhodococcus rhodochrous J1.
Nagasawa T., Takeuchi K., Yamada H.
A new cobalt-containing nitrile hydratase was purified from extracts of urea-induced cells from Rhodococcus rhodochrous J1 in seven steps. At the last step, the enzyme was crystallized by adding ammonium sulfate. Nitrile hydratase was a 500-530-kDa protein composed of two different subunits (alpha ... >> More
A new cobalt-containing nitrile hydratase was purified from extracts of urea-induced cells from Rhodococcus rhodochrous J1 in seven steps. At the last step, the enzyme was crystallized by adding ammonium sulfate. Nitrile hydratase was a 500-530-kDa protein composed of two different subunits (alpha subunit 26 kDa, beta subunit 29 kDa). The enzyme contained approximately 11-12 mol cobalt/mol enzyme. A concentrated solution of highly purified nitrile hydratase exhibited a broad absorption spectrum in the visible range, with an absorption maxima at 410 nm. The enzyme had a wide substrate specificity. Aliphatic saturated or unsaturated nitriles as well as aromatic nitriles, were substrates for the enzyme. The optimum pH of the hydratase was pH 6.5-6.8. The enzyme was more stable than ferric nitrile hydratases. The amino-terminal sequence of each subunit of R. rhodochrous J1 enzyme was determined and compared with that of ferric nitrile hydratases. Prominent similarities were observed with the beta subunit. However, the amino acid sequence of the alpha subunit from R. rhodochrous J1 was quite different from that of the ferric enzymes. << Less
Eur. J. Biochem. 196:581-589(1991) [PubMed] [EuropePMC]
This publication is cited by 14 other entries.
Comments
Published in: Asano Y., Fujishiro K., Tani Y., Yamada H. (1992) Aliphatic Nitrile Hydratase from Arthrobacter sp. J-1 Purification and Characterization. Agric. Biol. Chem. 46: 1165-1174. DOI:10.1271/bbb1961.46.1165