β-Galactosidases (Escherichia coli) with Double Substitutions Show That Tyr-503 Acts Independently of Glu-461 but Cooperatively with Glu-537

Journal of Protein Chemistry

Volumn 22, Issue 7-8, 2003, Pages 663-668

  Roth, Nathan J ^a   Penner, Robert M ^a   Huber, Reuben E ^a  

^a UNIVERSITY OF CALGARY   (Canada)

Author keywords

galactosidase; Glutamic; Mechanism; Tyrosine

Indexed keywords

BACTERIAL ENZYME; BETA GALACTOSIDASE; GLUTAMIC ACID; TYROSINE;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CATALYST; CIRCULAR DICHROISM; CORRELATION ANALYSIS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME MECHANISM; ENZYME SUBUNIT; ESCHERICHIA COLI; NONHUMAN; PROTEIN DETERMINATION;

BETA-GALACTOSIDASE; BINDING SITES; CIRCULAR DICHROISM; ENZYME ACTIVATION; ENZYME STABILITY; ESCHERICHIA COLI; GALACTOSE; GLUTAMIC ACID; GLYCEROL; HEAT; METHANOL; MUTAGENESIS, SITE-DIRECTED; TYROSINE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 55449122765     PISSN: 02778033     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:JOPC.0000008731.16884.22     Document Type: Article

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