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Titolo:
Post-translational modification is essential for catalytic activity of nitrile hydratase
Autore:
Murakami, T; Nojiri, M; Nakayama, H; Odaka, M; Yohda, M; Dohmae, N; Takio, K; Nagamune, T; Endo, I;
Indirizzi:
RIKEN, Inst Phys & Chem Res, Biochem Syst Lab, Wako, Saitama 3510198, Japan RIKEN Wako Saitama Japan 3510198 m Syst Lab, Wako, Saitama 3510198, Japan Univ Tokyo, Sch Engn, Dept Chem & Biotechnol, Bunkyo Ku, Tokyo 1138656, Japan Univ Tokyo Tokyo Japan 1138656 otechnol, Bunkyo Ku, Tokyo 1138656, Japan Tokyo Univ Agr & Technol, Fac Technol, Dept Biotechnol & Life Sci, Koganei, Tokyo 1848588, Japan Tokyo Univ Agr & Technol Koganei Tokyo Japan 1848588 Tokyo 1848588, Japan
Titolo Testata:
PROTEIN SCIENCE
fascicolo: 5, volume: 9, anno: 2000,
pagine: 1024 - 1030
SICI:
0961-8368(200005)9:5<1024:PMIEFC>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
RHODOCOCCUS SP N-771; NONHEME IRON CENTER; BINDING ACTIVITY INVITRO; ESCHERICHIA-COLI; REDOX REGULATION; POSTTRANSLATIONAL MODIFICATION; NUCLEOTIDE-SEQUENCE; CRYSTAL-STRUCTURE; CYSTEINE RESIDUE; ENZYME CATALYSIS;
Keywords:
cysteine-sulfenic acid; cysteine-sulfinic acid; nitrile hydration; nonheme iron; oxidation; post-translational modification;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: Odaka, M RIKEN, Inst Phys & Chem Res, Biochem Syst Lab, Hirosawa 2-1, Wako, Saitama3510198, Japan RIKEN Hirosawa 2-1 Wako Saitama Japan 3510198 itama3510198, Japan
Citazione:
T. Murakami et al., "Post-translational modification is essential for catalytic activity of nitrile hydratase", PROTEIN SCI, 9(5), 2000, pp. 1024-1030

Abstract

Nitrile hydratase from Rhodococcus sp. N-771 is an alpha beta heterodimer with a nonheme ferric iron in the catalytic center. In the catalytic center, alpha Cys112 and alpha Cys114 are modified to a cysteine sulfinic acid (Cys-SO2H) and a cysteine sulfenic acid (Cys-SOH), respectively. To understand the function and the biogenic mechanism of these modified residues, we reconstituted the nitrile hydratase from recombinant unmodified subunits. Thealpha beta complex reconstituted under argon exhibited no activity. However, it gradually gained the enzymatic activity through aerobic incubation. ESI-LC/MS analysis showed that the anaerobically reconstituted alpha beta complex did not have the modification of alpha Cys112-SO2H and aerobic incubation induced the modification. The activity of the reconstituted alpha betacomplex correlated with the amount of alpha Cys112-SO2H. Furthermore, ESI-LC/MS analyses of the tryptic digest of the reconstituted complex. removed of ferric iron at low pH and carboxamidomethylated without reduction, suggested that alpha Cys114 is modified to Cys-SOH together with the sulfinic acid modification of alpha Cys112. These results suggest that alpha Cys112 and alpha Cys114 are spontaneously oxidized to Cys-SO2H and Cys-SOH, respectively, and alpha Cys112-SO2H is responsible for the catalytic activity solely or in combination with alpha Cys114-SOH.

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Documento generato il 26/01/20 alle ore 10:08:59