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Showing 1 to 20 of 154 for “"decarboxylase"”.

  1. Comparative analysis of Anopheles gambiae L-tyrosine decarboxylase and L-DOPA decarboxylase

    … and DOPA, respectively. Although tyrosine decarboxylase (TDC) has been mentioned in some reports, it has never been critically analyzed. The high sequence identity shared by tyrosine decarboxylase and DOPA decarboxylase in insects, and the similar structures of the substrates, tyrosine and …

    vt Repository record for Comparative analysis of Anopheles gambiae L-tyrosine decarboxylase and L-DOPA decarboxylase (opens in a new tab)

  2. Identification of pyruvate decarboxylase/indole pyruvate decarboxylase gene family members from Arabidopsis thaliana.

    … metabolic enzymes, including pyruvate decarboxylase (PDC), indole pyruvate decarboxylase (IPDC), and acetohydroxy acid synthase. PDC is a critical enzyme in plant metabolism that regulates energy production especially during periods of anaerobic stress. IPDC has long been proposed as a …

    umn Repository record for Identification of pyruvate decarboxylase/indole pyruvate decarboxylase gene family members from Arabidopsis thaliana. (opens in a new tab)

  3. Probing the Mechanism of Oxalate Decarboxylase

    Oxalate decarboxylase (EC 4. 1. 1. 2 OxDC) from Bacillus subtilis is a manganese-dependent enzyme that catalyzes the cleavage of the chemically inactive C-C bond in oxalate to yield formate and carbon dioxide. A mechanism involving Mn(III) has been proposed for OxDC, however no clear spectroscopic …

    purdue-thes Repository record for Probing the Mechanism of Oxalate Decarboxylase (opens in a new tab)

  4. Probing the mechanism of Bacillus subtilis oxalate decarboxylase

    Oxalate decarboxylase (EC 4. 1. 1. 2 OxDC) from Bacillus subtilis is a manganese-dependent enzyme that catalyzes the cleavage of the chemically inactive C-C bond in oxalate to yield formate and carbon dioxide. A mechanism involving Mn(III) has been proposed for OxDC, however no clear spectroscopic …

    iupui Repository record for Probing the mechanism of Bacillus subtilis oxalate decarboxylase (opens in a new tab)

  5. The epigenetics and role of Dopa Decarboxylase in heart development

    … interference. Ddc_exonla codes for the Dopa Decarboxylase (Ddc) protein, which is predominately expressed in the developing myocardium, this points to a role in fetal heart development. The role of Ddc in cardiogenesis is explored using knockout mice lacking Ddc_exonla expression in heart. …

    kings Repository record for The epigenetics and role of Dopa Decarboxylase in heart development (opens in a new tab)

  6. Comparative studies of oxalyl-CoA decarboxylase produced by soil and ruminal bacteria

    The aim of this project was to identify an enzyme responsible for the metabolism of oxalate which would be suitable for degrading oxalate in the rumen, and clone and characterise that gene.

    adelaide Repository record for Comparative studies of oxalyl-CoA decarboxylase produced by soil and ruminal bacteria (opens in a new tab)

  7. Die Rolle der Phosphatidylserin Decarboxylase für die mitochondriale Phospholipid-Biosynthese in Arabidopsis thaliana

    Die durch Phosphatidylserin Decarboxylase (PSD) katalysierte Decarboxylierung von Phosphatidylserin (PS) zu Phosphatidylethanolamin (PE) ist für Mitochondrien in Hefe und Mäusen von essentieller Bedeutung. Im Rahmen der vorliegenden Dissertation wurde erstmals die Rolle dieses PE-Syntheseweges in …

    potsdam-diss Repository record for Die Rolle der Phosphatidylserin Decarboxylase für die mitochondriale Phospholipid-Biosynthese in Arabidopsis thaliana (opens in a new tab)

  8. Methylmalonyl -Coa Decarboxylase (Ygfg) for Escherichia Coli: A New Activity for the Crotonase Superfamily

    The E113Q mutant exhibited significantly larger isotope effect for both kcat and kcat/Km than wild-type, suggesting differences in reaction mechanism between wild type and E113Q. Although experimental difficulties encountered did not allow quantitative studies of stereochemistry of the MMDC …

    uiuc Repository record for Methylmalonyl -Coa Decarboxylase (Ygfg) for Escherichia Coli: A New Activity for the Crotonase Superfamily (opens in a new tab)

  9. Investigation of Substrate Specificity in Phosphate Binding Barrels and Mechanistic Studies of Orotidine Monophosphate Decarboxylase

    "Orotidine 5'-monophosphate decarboxylase from Methanobacterium thermoautotrophicum (MtOMPDC) catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) and uridine 5'-monophosphate (UMP) with an enormous rate acceleration, 1.8 x 1016 (kcat = 5 s-1, 25°C; knon = 2.8 x 1016 s-1), and …

    uiuc Repository record for Investigation of Substrate Specificity in Phosphate Binding Barrels and Mechanistic Studies of Orotidine Monophosphate Decarboxylase (opens in a new tab)

  10. The Role of S-Adenosylmethionine Decarboxylase on Regulation of Polyamine and Trypanothione Metabolism in Trypanosoma Brucei

    … characterized T. brucei S-adenosylmethionine decarboxylase (AdoMetDC), a key enzyme required for the synthesis of spermidine and trypanothione, and examined the role of AdoMetDC on the regulation of polyamine and trypanothione metabolism. The recombinant T. brucei AdoMetDC enzyme displays low …

    utswmed Repository record for The Role of S-Adenosylmethionine Decarboxylase on Regulation of Polyamine and Trypanothione Metabolism in Trypanosoma Brucei (opens in a new tab)

  11. Mechanistic Studies of the Decarboxylation Reaction of 1,3-Dimethylortic Acid: A Possible Mechanism for Orotate Decarboxylase

    Made available in DSpace on 2014-12-10T23:01:58Z (GMT). No. of bitstreams: 1 7500433.pdf: 4318318 bytes, checksum: b561e8b5c78d80616e1855d67017e6d2 (MD5) Previous issue date: 1974

    uiuc Repository record for Mechanistic Studies of the Decarboxylation Reaction of 1,3-Dimethylortic Acid: A Possible Mechanism for Orotate Decarboxylase (opens in a new tab)

  12. Regulation of the speC gene encoding ornithine decarboxylase in Escherichia coli by putrescine, spermidine and cAMP

    … the speC gene encodes biosynthetic ornithine decarboxylase (ODC), an enzyme that catalyzes the decarboxylation of ornithine to produce putrescine. The two polyamines, putrescine and spermidine, and the cyclic AMP (CAMP) - cAMP receptor protein (CRP) are known to inhibit the expression of ODC …

    vt Repository record for Regulation of the speC gene encoding ornithine decarboxylase in Escherichia coli by putrescine, spermidine and cAMP (opens in a new tab)

  13. Functional and structural characterization of the mevalonate diphosphate decarboxylase and the isopentenyl diphosphate isomerase from Enterococcus faecalis

    … faecalis;</em> one is the mevalonate diphosphate decarboxylase (MDD) in the mevalonate pathway, and the other one is the isopentenyl diphosphate isomerase (IDI), which is downstream of MDD. Functional and structural studies on the mevalonate diphosphate decarboxylase from <em>Enterococcus …

    purdue-thes Repository record for Functional and structural characterization of the mevalonate diphosphate decarboxylase and the isopentenyl diphosphate isomerase from Enterococcus faecalis (opens in a new tab)

  14. In Search of Catalytic Proficiency: The Importance of Enzyme Conformational Change to Orotidine 5'-Monophosphate Decarboxylase Catalysis

    By applying the tools of enzymology learned in the Gerlt Laboratory and working successfully with numerous collaborators, I have furthered our understanding of the mechanism of one of Nature's best catalysts, OMPDC. Increasingly in enzymology, the role of conformational change in enzyme catalysis …

    uiuc Repository record for In Search of Catalytic Proficiency: The Importance of Enzyme Conformational Change to Orotidine 5'-Monophosphate Decarboxylase Catalysis (opens in a new tab)

  15. In search of catalytic proficiency: The importance of enzyme conformational change to orotidine 5’-monophosphate decarboxylase catalysis

    … biosynthesis, orotidine 5’-monophosphate decarboxylase (OMPDC). OMPDC catalyzes the decarboxylation of OMP to UMP; the uncatalyzed rate for this reaction has been estimated to be 2.8 x 1016 s-1 (1). The slow rate without OMPDC is attributable to the lack of internal stabilization of the …

    uiuc Repository record for In search of catalytic proficiency: The importance of enzyme conformational change to orotidine 5’-monophosphate decarboxylase catalysis (opens in a new tab)

  16. Investigations into the mechanism of orotidine 5'-monophosphate decarboxylase: Sources of substrate destabilization and transition state stabilization

    Orotidine 5′-monophosphate decarboxylase (OMPDC) achieves a rarely paralleled rate acceleration, yet the catalytic basis prompting this enhancement have yet to be fully elucidated. To accomplish decarboxylation, OMPDC must overcome the high energy barrier due to the localized anionic charge of the …

    uiuc Repository record for Investigations into the mechanism of orotidine 5'-monophosphate decarboxylase: Sources of substrate destabilization and transition state stabilization (opens in a new tab)

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