Primary structure of a cerulenin-binding. beta. -ketoacyl-(acyl carrier protein) synthase from barley chloroplasts
- Carlsberg Lab., Copenhagen (Denmark)
- Carlsberg Lab., Copenhagen (Denmark) Univ. of Copenhagen (Denmark)
The radioactively labeled {beta}-ketoacyl thioester synthase inhibitor ({sup 3}H)cerulenin was used to tag three dimeric barley chloroplast proteins ({alpha}{alpha}, {alpha}{beta}, and {beta}{beta}) from the stromal fraction. Oligonucleotides corresponding to amino acid sequences obtained from the purified proteins were used to generate with the polymerase chain reaction a probe for cDNAs encoding the {beta} subunit. cDNA sequencing revealed an open reading frame for 462 residues comprising the mature protein and a 35-amino acid transit peptide. The deduced amino acid sequence of the mature protein is homologous to the {beta}-ketoacyl-(acyl carrier protein) (ACP) synthase I (3-oxoacyl-ACP synthase; acyl-ACP:malonyl-ACP C-acyltransferase (decarboxylating), EC 2.3.1.41) of Escherichia coli. Under analogous experimental conditions ({sup 3}H)cerulenin tagged a single dimeric protein from spinach chloroplasts.
- OSTI ID:
- 6097198
- Journal Information:
- Proceedings of the National Academy of Sciences of the United States of America; (United States), Vol. 88:10; ISSN 0027-8424
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
CHLOROPHYLL-BINDING PROTEINS
AUTORADIOGRAPHY
OLIGONUCLEOTIDES
DNA SEQUENCING
AMINO ACID SEQUENCE
CHLOROPLASTS
DNA POLYMERASES
ENZYME INHIBITORS
ESCHERICHIA COLI
GENE AMPLIFICATION
SPINACH
TRANSFERASES
TRITIUM COMPOUNDS
BACTERIA
CELL CONSTITUENTS
ENZYMES
FOOD
HYDROGEN COMPOUNDS
MAGNOLIOPHYTA
MAGNOLIOPSIDA
MICROORGANISMS
MOLECULAR STRUCTURE
NUCLEIC ACIDS
NUCLEOTIDYLTRANSFERASES
ORGANIC COMPOUNDS
PHOSPHORUS-GROUP TRANSFERASES
PHOTOSYNTHETIC REACTION CENTERS
PLANTS
POLYMERASES
PROTEINS
STRUCTURAL CHEMICAL ANALYSIS
VEGETABLES
550201* - Biochemistry- Tracer Techniques