Wild-type and feedback-resistant phosphoribosyl pyrophosphate synthetases from Bacillus amyloliquefaciens: Purification, characterization, and application to increase purine nucleoside production

Applied Microbiology and Biotechnology

Volumn 93, Issue 5, 2012, Pages 2023-2033

  Zakataeva, Natalia P ^a   Romanenkov, Dmitriy V ^a   Skripnikova, Victoria S ^a   Vitushkina, Maria V ^a   Livshits, Vitaliy A ^a,b   Kivero, Alexandr D ^a   Novikova, Anna E ^a  

^a Ajinomoto Genetika Research Institute   (Russian Federation)

^b PEOPLES FRIENDSHIP UNIVERSITY OF RUSSIA   (Russian Federation)

Author keywords

Bacillus amyloliquefaciens; Bacillus subtilis; Feedback resistance; Phosphoribosyl pyrophosphate synthetase; Purine nucleoside producing strains

Indexed keywords

BACILLUS AMYLOLIQUEFACIENS; BACILLUS STRAIN; BACILLUS SUBTILIS; CLASS I; DIPHOSPHATES; END-PRODUCTS; ENZYMATIC PROPERTIES; FEEDBACK RESISTANCE; GUANOSINES; INDUSTRIAL PRODUCTION; INORGANIC PHOSPHATES; INOSINE; SYNTHETASES; URIC ACIDS; WILD TYPES; WILD-TYPE PROTEINS;

AMINO ACIDS; BACTERIOLOGY; BIOCHEMISTRY; ENZYME INHIBITION; ESCHERICHIA COLI; PURIFICATION;

BIOMOLECULES;

ADENOSINE DIPHOSPHATE; GUANOSINE DIPHOSPHATE; PHOSPHATE; PURINE NUCLEOSIDE; PURINE NUCLEOTIDE; RIBOSEPHOSPHATE PYROPHOSPHOKINASE;

BACTERIUM; ENZYME ACTIVITY; MUTATION; PURIFICATION; WILD POPULATION;

AMINO ACID SEQUENCE; ARTICLE; BACILLUS AMYLOLIQUEFACIENS; BACTERIAL GROWTH; CONTROLLED STUDY; ENZYME ANALYSIS; ENZYME PURIFICATION; GENE MUTATION; GLUCOSE INTAKE; HETEROLOGOUS EXPRESSION; MOLECULAR CLONING; NUCLEOTIDE SEQUENCE; PROTEIN EXPRESSION;

ADENOSINE DIPHOSPHATE; AMINO ACID SUBSTITUTION; BACILLUS; CLONING, MOLECULAR; ENZYME INHIBITORS; ESCHERICHIA COLI; GENE EXPRESSION; GUANOSINE; GUANOSINE DIPHOSPHATE; INOSINE; MOLECULAR SEQUENCE DATA; MUTANT PROTEINS; MUTATION, MISSENSE; PHOSPHORIBOSYL PYROPHOSPHATE; RIBOSE-PHOSPHATE PYROPHOSPHOKINASE; SEQUENCE ANALYSIS, DNA;

BACILLUS AMYLOLIQUEFACIENS; BACILLUS SUBTILIS; ESCHERICHIA COLI; MAMMALIA;

EID: 84857920641     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-011-3687-3     Document Type: Article

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