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Volumn 130, Issue 36, 2008, Pages 11939-11944

Hydroxylase activity of Met471Cys tyramine β-monooxygenase

Author keywords

[No Author keywords available]

Indexed keywords

HYDROXYLASE ACTIVITY; MONOOXYGENASE;

EID: 51749083478     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja800408h     Document Type: Article
Times cited : (25)

References (22)
  • 13
    • 0030766385 scopus 로고    scopus 로고
    • While CHO cell lines containing Met314Cys and Met314His PHM mutations also have been reported Kolhekar, A. S, Keutmann, H. T, Mains, R. E, Quon, A. S. W, Eipper, B. A. Biochemistry 1997, 36, 10901-10909, neither of the mutant proteins was isolated and structurally characterized, and activity assays were carried out with spent media rather than using purified protein
    • While CHO cell lines containing Met314Cys and Met314His PHM mutations also have been reported (Kolhekar, A. S.; Keutmann, H. T.; Mains, R. E.; Quon, A. S. W.; Eipper, B. A. Biochemistry 1997, 36, 10901-10909.), neither of the mutant proteins was isolated and structurally characterized, and activity assays were carried out with spent media rather than using purified protein.
  • 17
    • 51749104197 scopus 로고    scopus 로고
    • Deviations from the double integration values of original spectrum were within ±25%, with the largest deviation obtained for WT TβM; therefore, the discrepancies likely arise from differences in standard integration values on different days, as well as due to some loss of Cu and/or protein due to handling/freeze-thawing of the samples.
    • Deviations from the double integration values of original spectrum were within ±25%, with the largest deviation obtained for WT TβM; therefore, the discrepancies likely arise from differences in standard integration values on different days, as well as due to some loss of Cu and/or protein due to handling/freeze-thawing of the samples.
  • 18
    • 51749112272 scopus 로고    scopus 로고
    • Substrate turnover by WT TβM also was measured independently in a separate assay measuring oxygen consumption by the enzyme. The latter assay provides a more precise measure of initial rates, compared to HPLC analysis. The kcat value obtained for the oxygen electrode assay (kcat, 3.3 s-1) under identical conditions is comparable to the value obtained by monitoring octopamine formation by HPLC
    • -1) under identical conditions is comparable to the value obtained by monitoring octopamine formation by HPLC.
  • 20


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.