Amino acid sequence of the biotinyl subunit from transcarboxylase.

Maloy, W L; Bowien, Botho; Zwolinski, Gene K.; Kumar, K.G.; Wood, Harland G.; Ericsson, Lowell H.; Walsh, Kenneth A.

doi:10.1016/s0021-9258(19)86529-8

Cited by 53 publications

(11 citation statements)

References 21 publications

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“…Amino acid residues corresponding to the numbering in the sequence motifs are in boldface. Sequences were taken from the references indicated: human PYC (67); M. tuberculosis PYC (57); P. shermanii TC 5s subunit (64); human propionyl-CoA carboxylase (PCC) ␣ subunit (31); rat carbamylphosphate synthase (CPS) (44); E. coli ACC BC subunit (32); E. coli ACC BCCP subunit (41); and P. shermanii TC 1.3s subunit (35).…”

Section: Discussionmentioning

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: Discussionmentioning

confidence: 99%

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

et al. 1996

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“…The 1.3Se subunit is not a globular protein (Wood et al, 1975) and is unusual since it does not contain tryptophan. Of its 123 residues only one is tyrosine and only one is phenylalanine (Maloy et al, 1979). This protein also contains biotin.…”

Section: Discussionmentioning

confidence: 99%

“…The biotinyl subunit contains 123 residues and its sequence has been determined (Maloy et al, 1979). It has recently been shown that attachment of the outside subunits to the central 12Sh subunit is via residues 1-23 and another portion is involved in orienting the biotin at the substrate sites (Kumar & Beegen, 1981).…”

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confidence: 99%

Subunit interactions of transcarboxylase as studied by circular dichroism

Hennessey¹,

Johnson²,

Bahler³

et al. 1982

Biochemistry

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A change in the secondary structure of transcarboxylase from quaternary interactions is monitored by circular dichroism spectroscopy. The change is traced to interactions among the six polypeptides that make up the 12SH subunit. It is fully reversible and is not a result of the conditions used to dissociate the enzyme. Our new method of analyzing circular dichroism spectra for secondary structure works well for this enzyme and its subunits. Even the odd circular dichroism of the 1.3SE subunit analyzes well. There is an increase of 19% in alpha helix and a concomitant decrease of 8% in antiparallel beta sheet and 7% in random structure on association to form the hexameric 12SH subunit.

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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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Amino acid sequence of the biotinyl subunit from transcarboxylase.

Cited by 53 publications

References 21 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

Subunit interactions of transcarboxylase as studied by circular dichroism

Structure, function and regulation of pyruvate carboxylase

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