Structural classification of biotin carboxyl carrier proteins
نویسندگان
چکیده
منابع مشابه
Biotin carboxyl carrier protein isoforms in Brassicaceae oilseeds.
De novo fatty acid biosynthesis occurs predominantly in plastids. The committed step for this pathway is the production of malonyl-CoA catalysed by acetyl-CoA carboxylase (ACCase). In most plants, plastidial ACCase is a multisubunit complex minimally comprised of four polypeptides, which catalyse two reactions. In the simple oilseed plant, Arabidopsis thaliana, two cDNAs encoding biotin carboxy...
متن کاملThe biotin carboxylase-biotin carboxyl carrier protein complex of Escherichia coli acetyl-CoA carboxylase.
Escherichia coli acetyl-CoA carboxylase (ACC) is composed of four different protein molecules. These proteins form a large but very unstable complex. Hints of a sub-complex between the biotin carboxylase (BC) and biotin carboxyl carrier protein (BCCP) subunits have been reported in the literature, but the complex was not isolated and thus the protein stoichiometry could not be determined. We re...
متن کاملAcetyl coenzyme A carboxylase. Proteolytic modification of biotin carboxyl carrier protein.
The biotin carboxyl carrier protein (BCCP) component of Escherichia coli acetyl coenzyme A carboxylase has been previously isolated in multiple active forms, ranging in molecular weight from 45,000 to 9,100. Since the apparent native form of BCCP is the largest of these species, the isolation of the small forms was attributed to proteolysis during the purification procedures employed. We have n...
متن کاملBrassicaceae express multiple isoforms of biotin carboxyl carrier protein in a tissue-specific manner.
Plastidial acetyl-coenzyme A carboxylase from most plants is a multi-enzyme complex comprised of four different subunits. One of these subunits, the biotin carboxyl carrier protein (BCCP), was previously proposed to be encoded by a single gene in Arabidopsis. We report and characterize here a second Arabidopsis BCCP (AtBCCP2) cDNA with 42% amino acid identity to AtBCCP1 and 75% identity to a cl...
متن کاملPurification and characterization of intact and truncated forms of the Escherichia coli biotin carboxyl carrier subunit of acetyl-CoA carboxylase.
Biotin biosynthesis and retention in Escherichia coli is regulated by the multifunctional protein, BirA. The protein acts as both the transcriptional repressor of the biotin biosynthetic operon and as a ligase for covalent attachment of biotin to a unique lysine residue of the acetyl-CoA carboxylase. Biotinyl-5'-AMP is the activated intermediate for the ligase reaction and the allosteric effect...
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ژورنال
عنوان ژورنال: Biotechnology Letters
سال: 2012
ISSN: 0141-5492,1573-6776
DOI: 10.1007/s10529-012-0978-4