Evidence from proteomics that some of the enzymes of actinorhodin biosynthesis have more than one form and may occupy distinctive cellular locations

Journal of Industrial Microbiology and Biotechnology

Volumn 30, Issue 8, 2003, Pages 523-529

  Hesketh, Andrew ^a   Chater, Keith F ^a  

^a JOHN INNES CENTRE   (United Kingdom)

Author keywords

2D gel electrophoresis; Polyketides; Proteolytic processing; Secondary metabolism

Indexed keywords

ACTINORHODINE; BACTERIAL PROTEIN; GENE PRODUCT; POLYKETIDE; PROTEIN ACT; PYRAN DERIVATIVE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ANTIBIOTIC BIOSYNTHESIS; BIOTECHNOLOGICAL PRODUCTION; CONFERENCE PAPER; CONTROLLED STUDY; COVALENT BOND; GENE CLUSTER; GENE LOCATION; GENE MAPPING; GENE TECHNOLOGY; GENETIC ENGINEERING; NONHUMAN; NUCLEOTIDE SEQUENCE; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROCESSING; PROTEOMICS; RING CLOSING METATHESIS; STREPTOMYCES COELICOLOR; TWO DIMENSIONAL GEL ELECTROPHORESIS;

3-HYDROXYACYL COA DEHYDROGENASES; ACYLTRANSFERASES; AMINO ACID SEQUENCE; ANTHRAQUINONES; BACTERIAL PROTEINS; ELECTROPHORESIS, GEL, TWO-DIMENSIONAL; INDUSTRIAL MICROBIOLOGY; MACROLIDES; MOLECULAR SEQUENCE DATA; MULTIENZYME COMPLEXES; OPEN READING FRAMES; OXIDOREDUCTASES; POLYKETIDE SYNTHASES; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEOMICS; STREPTOMYCES;

ACTINOBACTERIA (CLASS); BACTERIA (MICROORGANISMS); STREPTOMYCES; STREPTOMYCES COELICOLOR; UNCULTURED ACTINOMYCETE;

EID: 0141817742     PISSN: 13675435     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10295-003-0067-8     Document Type: Conference Paper

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