2001
DOI: 10.1016/s0162-0134(00)00171-9
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Fe-type nitrile hydratase

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Cited by 124 publications
(91 citation statements)
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“…We assume that the two cysteine residues (␣Cys 111 and ␣Cys 113 ) are posttranslationally oxidized to cysteine-sulfinic acid and cysteine-sulfenic acid, after expression in E. coli. Spontaneous oxidization of a recombinant Fe-type NHase has also been reported (23 Table 2). These arginine residues are conserved in all known NHases.…”
Section: Structure Of the Active Centermentioning
confidence: 90%
“…We assume that the two cysteine residues (␣Cys 111 and ␣Cys 113 ) are posttranslationally oxidized to cysteine-sulfinic acid and cysteine-sulfenic acid, after expression in E. coli. Spontaneous oxidization of a recombinant Fe-type NHase has also been reported (23 Table 2). These arginine residues are conserved in all known NHases.…”
Section: Structure Of the Active Centermentioning
confidence: 90%
“…Activation of the C N bond occurs through coordination to the metal atom, thus enhancing the rate of the hydration step. [6,7] However, despite the high number of metal-mediated hydration of nitriles reported to date, only a few complexes can act as selective catalysts to form amides.…”
mentioning
confidence: 99%
“…While the Co-and Fe-type NHases from different organisms are significantly homologous at the amino acid level there are substantial differences at the genetic level (Kobayashi et al , 1993Komeda et al 1996;O'Mahony et al 2005). Of particular significance to this current study is the presence of an ORF in all Fetype NHase gene clusters analysed to date, encoding a protein named P47k or P44k depending on the source organism Endo et al 2001;O'Mahony et al 2005). The P47k protein is essential for active expression in E. coli of the NHases of Rhodococcus sp.N771 and N774 and Pseudomonas chlororaphis B23 (Hashimoto et al 1994;Nojiri et al 1999;Goda et al 2002).…”
Section: Introductionmentioning
confidence: 91%