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Volumn 303, Issue 2, 2000, Pages 279-286

Identification of an allosteric anion-binding site on O-acetylserine sulfhydrylase: Structure of the enzyme with chloride bound

Author keywords

Allosteric inhibition; Conformational change; Cysteine biosynthesis; O acetylserine sulfhydrylase; Pyridoxal 5'phosphate

Indexed keywords

ANION; CHLORIDE; CYSTEINE; CYSTEINE SYNTHASE; SCHIFF BASE; SULFIDE;

EID: 0034692879     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.4109     Document Type: Article
Times cited : (70)

References (29)
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    • A reaction mechanism from steady state kinetic studies for O-acetylserine sulfhydrylase from Salmonella typhimurium LT-2
    • (1976) J. Biol. Chem. , vol.251 , pp. 2023-2029
    • Cook, P.F.1    Wedding, R.T.2
  • 16
    • 0004113645 scopus 로고
    • Joint CCP4 + ESF-EAMCB Newsletter on Protein Crystallography
    • (1992) , vol.26
    • Leslie, A.G.W.1
  • 17
    • 0028174296 scopus 로고
    • Product binding to the α-carboxyl subsite results in a conformational change at the active site of O-acetylserine sulfhydrylase-A: Evidence from fluorescence spectroscopy
    • (1994) Biochemistry , vol.33 , pp. 1674-1683
    • McClure G.D., Jr.1    Cook, P.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.