Three of four cysteines, including that responsible for substrate activation, are ionized at pH 6.0 in yeast pyruvate decarboxylase: Evidence from Fourier transform infrared and isoelectric focusing studies

Biochemistry

Volumn 35, Issue 32, 1996, Pages 10249-10255

  Baburina, Irina ^a   Moore, David J ^a   Volkov, Alexander ^a   Kahyaoglu, Ara ^a   Jordan, Frank ^a   Mendelsohn, Richard ^a  

^a RUTGERS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PYRUVATE DECARBOXYLASE;

AMINO ACID SEQUENCE; ARTICLE; ENZYME ACTIVE SITE; ENZYME SUBSTRATE COMPLEX; FOURIER ANALYSIS; ISOELECTRIC FOCUSING; NONHUMAN; PRIORITY JOURNAL; SACCHAROMYCES CEREVISIAE;

CYSTEINE; DNA PRIMERS; ENZYME ACTIVATION; HYDROGEN-ION CONCENTRATION; ISOELECTRIC FOCUSING; MUTAGENESIS, SITE-DIRECTED; PYRUVATE DECARBOXYLASE; SACCHAROMYCES CEREVISIAE; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; SUBSTRATE SPECIFICITY;

SACCHAROMYCES CEREVISIAE;

EID: 0029797722     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi961141+     Document Type: Article

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