Cysteine 195 has a critical functional role in catalysis by isocitrate lyase from Escherichia coli

Current Microbiology

Volumn 35, Issue 5, 1997, Pages 267-269

  Rehman, Abdur ^a   McFadden, Bruce A ^a  

^a WASHINGTON STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; CYSTEINE; ISOCITRATE LYASE;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; ENZYME ACTIVITY; ENZYME MODIFICATION; ESCHERICHIA COLI; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL;

ALANINE; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; CYSTEINE; ESCHERICHIA COLI; GLYCINE; ISOCITRATE LYASE; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PLASMIDS; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY, AMINO ACID; SERINE; THREONINE; VALINE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; FELIS CATUS;

EID: 0030721646     PISSN: 03438651     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002849900251     Document Type: Article

References (12)

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9. Rehman A, McFadden BA (1997a) Serine 319 and 321 are functional in isocitrate lyase from Escherichia coli. Curr Microbiol, in press.
10. Rehman A, McFadden BA (1997b) Lysine 194 is functional in isocitrate lyase from Escherichia coli. Curr Microbiol, in press.
11. Robertson AGS, Nimmo HG (1995) Site-directed mutagenesis of cysteine-195 in isocitrate lyase from Escherichia coli ML308. Biochem J 305:239-244
12. Vanni P, Giachetti G, Pinzauti G, McFadden BA (1990) Comparative structure, function, and regulation of isocitrate lyase, an important assimilatory enzyme. Comp Biochem Physiol B 95:431-458