The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase.

Li, Shyr-Jiann; Cronan, John E.

doi:10.1016/s0021-9258(18)48362-7

Cited by 205 publications

(30 citation statements)

References 56 publications

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“…7) and in the ␣ subunit of propionyl-CoA carboxylase (Fig. 8), a PX(P/A) sequence occurs; this sequence is proposed to be involved in the recognition and biotinylation of the biotin carboxylases (32).…”

Section: Resultsmentioning

confidence: 99%

Pyruvate carboxylase from Rhizobium etli: mutant characterization, nucleotide sequence, and physiological role

et al. 1996

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Pyruvate carboxylase (PYC), a biotin-dependent enzyme which catalyzes the conversion of pyruvate to oxaloacetate, was hypothesized to play an important anaplerotic role in the growth of Rhizobium etli during serial subcultivation in minimal media containing succinate (S. Encarnación, M. Dunn, K. Willms, and J. Mora, J. Bacteriol. 177:3058-3066, 1995). R. etli and R. tropici pyc::Tn5-mob mutants were selected for their inability to grow in minimal medium with pyruvate as a sole carbon source. During serial subcultivation in minimal medium containing 30 mM succinate, the R. etli parent and pyc mutant strains exhibited similar decreases in growth rate with each subculture. Supplementation of the medium with biotin prevented the growth decrease of the parent but not the mutant strain, indicating that PYC was necessary for the growth of R. etli under these conditions. The R. tropici pyc mutant grew normally in subcultures regardless of biotin supplementation. The symbiotic phenotypes of the pyc mutants from both species were similar to those of the parent strains. The R. etli pyc was cloned, sequenced, and found to encode a 126-kDa protein of 1,154 amino acids. The deduced amino acid sequence is highly homologous to other PYC sequences, and the catalytic domains involved in carboxylation, pyruvate binding, and biotinylation are conserved. The sequence and biochemical data show that the R. etli PYC is a member of the alpha4, homotetrameric, acetyl coenzyme A-activated class of PYCs.

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Section: Resultsmentioning

confidence: 99%

Pyruvate carboxylase from Rhizobium etli: mutant characterization, nucleotide sequence, and physiological role

et al. 1996

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“…Biotinylation of BCCP is also thought to be possible both before and after assembly into acetyl-CoA carboxylase. Biotinylation studies on E. coli, chicken and human apoacetyl-CoA carboxylases [25][26][27], and on fusion proteins containing biotinyl domains [23,24], support this conclusion. This suggests that the biocytin 3 hairpin, notably Lys122, must be near the surface to facilitate biotinylation by BirA as well as the intersubunit translocation of the biotinyl moiety.…”

Section: Functional Interactions Of Bccpmentioning

confidence: 90%

“…Thus, bacterial holocarboxylase synthetase can biotinylate rat apocarboxylases [21,22]. Only the biotinyl domain of apocarboxylase is necessary for biotinylation [23,24], although synthetases can biotinylate intact apocarboxylases [25][26][27]. Thus, we expect that an analysis of biotinylation of BCCPsc by the E. coli holocarboxylase synthetase (BirA) [25,28], the structure of which is known [29], will enhance our understanding of biotinylation in man.…”

Section: Introductionmentioning

confidence: 99%

Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing

1995

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This first crystal structure of a biotinyl domain helps to unravel the central role of such domains in reactions catalyzed by biotin-dependent carboxylases. The hammerhead structure observed twice in BCCPsc may be regarded as the basic structural motif of biotinyl and lipoyl domains of a superfamily of enzymes. The new MAD phasing techniques developed in the course of determining this structure enhance the power of the MAD method.

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“…thermo.) [47] ; ACC human [117] ; ACC S. cerevisiae [118] ; ACC E. coli [119] ; CPS E. coli [120], CPS S. cerevisiae [121] ; transcarboxylase (TC), 5 S subunit [122] and 1.3 S subunit [123] of P. shermanii ; ODCα (oxaloacetate decarboxylase α-subunit) Klebsiella pneumoniae [124] ; ODCα Salmonella typhimurium [125] ; PCCα (PCC α-subunit) human [126] ; 3-hydroxyl-3-methylglutaryl-CoA lyase (HMG-lyase) rat (Rattus norvegicus) [127] ; HMG-lyase chicken (Gallus gallus) [128].…”

Section: Figure 1 Multiple Sequence Alignment Of Pc With Other Biotin-dependent Enzymesmentioning

confidence: 99%

Structure, function and regulation of pyruvate carboxylase

JITRAPAKDEE¹,

Wallace²

1999

Biochem. J.

114

103

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Pyruvate carboxylase (PC; EC 6.4.1.1), a member of the biotin-dependent enzyme family, catalyses the ATP-dependent carboxylation of pyruvate to oxaloacetate. PC has been found in a wide variety of prokaryotes and eukaryotes. In mammals, PC plays a crucial role in gluconeogenesis and lipogenesis, in the biosynthesis of neurotransmitter substances, and in glucose-induced insulin secretion by pancreatic islets. The reaction catalysed by PC and the physical properties of the enzyme have been studied extensively. Although no high-resolution three-dimensional structure has yet been determined by X-ray crystallography, structural studies of PC have been conducted by electron microscopy, by limited proteolysis, and by cloning and sequencing of genes and cDNA encoding the enzyme. Most well characterized forms of active PC consist of four identical subunits arranged in a tetrahedron-like structure. Each subunit contains three functional domains: the biotin carboxylation domain, the transcarboxylation domain and the biotin carboxyl carrier domain. Different physiological conditions, including diabetes, hyperthyroidism, genetic obesity and postnatal development, increase the level of PC expression through transcriptional and translational mechanisms, whereas insulin inhibits PC expression. Glucocorticoids, glucagon and catecholamines cause an increase in PC activity or in the rate of pyruvate carboxylation in the short term. Molecular defects of PC in humans have recently been associated with four point mutations within the structural region of the PC gene, namely Val145-->Ala, Arg451-->Cys, Ala610-->Thr and Met743-->Thr.

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The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase.

Cited by 205 publications

References 56 publications

Pyruvate carboxylase from Rhizobium etli: mutant characterization, nucleotide sequence, and physiological role

Pyruvate carboxylase from Rhizobium etli: mutant characterization, nucleotide sequence, and physiological role

Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing

Structure, function and regulation of pyruvate carboxylase

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