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Volumn 121, Issue 21, 1999, Pages 4977-4981

Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of cysteine mutants

Author keywords

[No Author keywords available]

Indexed keywords

AMIDASE; CYSTEINE; ESTERASE; MUTANT PROTEIN; SERINE PROTEINASE;

EID: 0033516322     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja9902266     Document Type: Article
Times cited : (24)

References (54)
  • 51
    • 0345264829 scopus 로고    scopus 로고
    • note
    • It was recognized that the cysteine thiol of the unmodified cysteine mutants N62C, L217C, S166C, and M222C could react with DTNB, which is used in the kinetic assay to detect the thiol benzyl hydrolysis product of the esterase reaction. This possibility was discounted by studying the rates of reaction of DTNB with N62C, S166C, L217C, and β-mercaptoethanol as a model for a nonhindered thiol, which established that these did not react at a rate sufficient to interfere with the assay at the concentrations used.
  • 52
    • 0344833434 scopus 로고    scopus 로고
    • note
    • M (amidase) for analogous ester and amide substrates, and in the few cases where this inequality does not hold, the rate-limiting step for ester hydroysis may have changed.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.