Primary amino acid sequence and structure of human pyruvate carboxylase

Wexler, Isaiah D.; Du, Yunpeng; Lisgaris, Michelle V.; Mandal, Sushim; Freytag, Svend O.; Yang, Beomjoo; Liu, Te Cheung; Kwon, Moosik; Patel, Mulchand S.; Kerr, Douglas S.

doi:10.1016/0925-4439(94)90105-8

Cited by 46 publications

(46 citation statements)

References 31 publications

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“…A homogenous sample of R. capsulatus PC, purified as described in Materials and Methods, was subjected to SDS-PAGE, and the N-terminal amino acid sequence of the PC polypeptide was determined by Edman degradation after transfer to a polyvinylidene difluoride membrane. The sequence was MFEKILVA NRGEIAIRVLRAANEL, which shows a high degree of similarity with the N-terminal regions of PCs from yeast and animals (18,20,22,35,41,48). The sequence is almost identical to that previously determined for R. capsulatus (24), with the only difference being in the seventh residue (underlined); it was Val in the sequence presented here and Met according to the data of Modak and Kelly (24 (18,20,22,35,41,48).…”

Section: Resultssupporting

confidence: 55%

“…The sequence was MFEKILVA NRGEIAIRVLRAANEL, which shows a high degree of similarity with the N-terminal regions of PCs from yeast and animals (18,20,22,35,41,48). The sequence is almost identical to that previously determined for R. capsulatus (24), with the only difference being in the seventh residue (underlined); it was Val in the sequence presented here and Met according to the data of Modak and Kelly (24 (18,20,22,35,41,48). Despite these minor differences, we believe that the protein isolated here is identical to that previously isolated (24).…”

Section: Resultsmentioning

confidence: 99%

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Regulation of synthesis of pyruvate carboxylase in the photosynthetic bacterium Rhodobacter capsulatus

Yakunin

Hallenbeck

1997

J Bacteriol

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The synthesis of pyruvate carboxylase (PC) was studied by using quantitative immunoblot analysis with an antibody raised against PC purified from Rhodobacter capsulatus and was found to vary 20-fold depending on the growth conditions. The PC content was high in cells grown on pyruvate or on carbon substrates metabolized via pyruvate (lactate, D-malate, glucose, or fructose) and low in cells grown on tricarboxylic acid (TCA) cycle intermediates or substrates metabolized without intermediate formation of pyruvate (acetate or glutamate). Under dark aerobic growth conditions with lactate as a carbon source, the PC content was approximately twofold higher than that found under light anaerobic growth conditions. The results of incubation experiments demonstrate that PC synthesis is induced by pyruvate and repressed by TCA cycle intermediates, with negative control dominating over positive control. The content of PC in R. capsulatus cells was also directly related to the growth rate in continuous cultures. The analysis of intracellular levels of pyruvate and TCA cycle intermediates in cells grown under different conditions demonstrated that the content of PC is directly proportional to the ratio between pyruvate and C 4 dicarboxylates. These results suggest that the regulation of PC synthesis by oxygen and its direct correlation with growth rate may reflect effects on the balance of intracellular pyruvate and C 4 dicarboxylates. Thus, this important enzyme is potentially regulated both allosterically and at the level of synthesis.

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Section: Resultssupporting

confidence: 55%

Section: Resultsmentioning

confidence: 99%

Regulation of synthesis of pyruvate carboxylase in the photosynthetic bacterium Rhodobacter capsulatus

Yakunin

Hallenbeck

1997

J Bacteriol

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“…7) revealed that the ATP binding motif and other sequence features, which are usually associated with the biotin carboxylases, were present in PYCA; note that we renamed the M. jannaschii BC as M. jannaschii PYCA for the reasons given under "Discussion." The sequence GGGGIGM-RAV of PYCA (residues 162-171) matched the consensus GGGGXGMRUU (U ϭ A, I, L, V) sequence that is implicated in binding ATP by biotin carboxylases (39,41,47). This consensus sequence is similar to the "P loop" motif GXXXXGK(TS) that is involved in binding ATP or the nucleotide portion of nicotinamides in several ATP-or nicotinamide-dependent enzymes (48,49).…”

Section: Purification and Molecular Properties Of Pyruvatementioning

confidence: 99%

Purification, Regulation, and Molecular and Biochemical Characterization of Pyruvate Carboxylase from Methanobacterium thermoautotrophicum Strain ΔH

Mukhopadhyay

Stoddard²,

Wolfe

1998

Journal of Biological Chemistry

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We discovered that Methanobacterium thermoautotrophicum strain ⌬H possessed pyruvate carboxylase (PYC), and this biotin prototroph required exogenously supplied biotin to exhibit detectable amounts of PYC activity. The enzyme was highly labile and was stabilized by 10% inositol in buffers to an extent that allowed purification to homogeneity and characterization. , or Co 2؉ . The 540-kDa enzyme of A 4 B 4 composition contained a non-biotinylated 52-kDa subunit (PYCA) and a 75-kDa biotinylated subunit (PYCB). The pycB gene was probably monocistronic and followed by a putative gene of a DNA-binding protein on the opposite strand. The pycA was about 727 kilobase pairs away from pycB on the chromosome and was probably co-transcribed with the biotin ligase gene (birA). PYCA and PYCB showed substantial sequence identities (33-62%) to, respectively, the biotin carboxylase and biotin carboxyl carrier ؉ carboxyltransferase domains or subunits of known biotin-dependent carboxylases/decarboxylases. We discovered that PYCB and probably the equivalent domains or subunits of all biotin-dependent carboxylases harbored the serine/ threonine dehydratase types of pyridoxal-phosphate attachment site. Our results and the existence of an alternative oxaloacetate synthesizing enzyme phosphoenolpyruvate carboxylase in M. thermoautotrophicum strain ⌬H (Kenealy, W. R., and Zeikus, J. G. (1982) FEMS Microbiol. Lett. 14, 7-10) raise several questions for future investigations.

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“…Genes encoding this enzyme in bacteria (7), yeast (8 -10), and cDNAs from mosquito (11), mouse (12), rat (13,14), and human (15,16) have been isolated and characterized. We have also identified and described multiple transcripts of rat and human PC mRNAs, which within the same species encode the same protein but diverge in their 5Ј-untranslated regions (5Ј-UTR) (17).…”

mentioning

confidence: 99%