Identification of arginine 331 as an important active site residue in the Class II fructose-1,6-bisphosphate aldolase of Escherichia coli

Protein Science

Volumn 5, Issue 1, 1996, Pages 154-161

  Qamar, Seema ^a,b   Marsh, Katherine ^a,c   Berry, Alan ^a,b  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b UNIVERSITY OF LEEDS   (United Kingdom)

^c NEWCASTLE UNIVERSITY   (United Kingdom)

Author keywords

aldolase; chemical modification; fructose bisphosphate; phenylglyoxal; protein engineering; substrate binding

Indexed keywords

BACTERIAL ENZYME; FRUCTOSE BISPHOSPHATE ALDOLASE;

ARTICLE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME BINDING; ENZYME INHIBITION; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0030070065     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560050119     Document Type: Article

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