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Volumn 57, Issue 3, 2001, Pages 363-367
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Replacement of arginine-171 and aspartate-453 in Streptomyces coelicolor malate synthase A by site-directed mutagenesis inactivates the enzyme
a a a |
Author keywords
[No Author keywords available]
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Indexed keywords
ACETYL COENZYME A;
ARGININE;
ASPARTIC ACID;
MAGNESIUM ION;
MALATE SYNTHASE;
MALATE SYNTHASE A;
MUTANT PROTEIN;
UNCLASSIFIED DRUG;
BIOTECHNOLOGY;
ENZYME;
AMINO ACID SUBSTITUTION;
ARTICLE;
CATALYSIS;
CONTROLLED STUDY;
ENZYME ACTIVITY;
ENZYME ANALYSIS;
ENZYME ASSAY;
ENZYME INACTIVATION;
ESCHERICHIA COLI;
NONHUMAN;
NUCLEOTIDE SEQUENCE;
PROTEIN EXPRESSION;
PROTEIN PURIFICATION;
SEQUENCE HOMOLOGY;
SITE DIRECTED MUTAGENESIS;
STREPTOMYCES COELICOLOR;
AMINO ACID SEQUENCE;
AMINO ACID SUBSTITUTION;
ARGININE;
ASPARTIC ACID;
ELECTROPHORESIS, POLYACRYLAMIDE GEL;
ENZYME ACTIVATION;
ESCHERICHIA COLI;
MALATE SYNTHASE;
MOLECULAR SEQUENCE DATA;
MUTAGENESIS, SITE-DIRECTED;
SEQUENCE HOMOLOGY, AMINO ACID;
STREPTOMYCES;
ACTINOBACTERIA (CLASS);
ESCHERICHIA COLI;
NEGIBACTERIA;
STREPTOMYCES COELICOLOR;
UNCULTURED ACTINOMYCETE;
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EID: 0034787623
PISSN: 01757598
EISSN: None
Source Type: Journal
DOI: 10.1007/s002530100785 Document Type: Article |
Times cited : (2)
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References (11)
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