Oxaloacetate decarboxylase
Oxaloacetate decarboxylase structure
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Common Name | Oxaloacetate decarboxylase | ||
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| CAS Number | 9024-98-0 | Molecular Weight | N/A | |
| Density | N/A | Boiling Point | N/A | |
| Molecular Formula | N/A | Melting Point | N/A | |
| MSDS | USA | Flash Point | N/A | |
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Functionally diverse biotin-dependent enzymes with oxaloacetate decarboxylase activity.
Arch. Biochem. Biophys. 544 , 75-86, (2014) Biotin-dependent enzymes catalyze carboxylation, decarboxylation and transcarboxylation reactions that participate in the primary metabolism of a wide range of organisms. In all cases, the overall reaction proceeds via two half reactions that take place in ph... |
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Kinetic challenges facing oxalate, malonate, acetoacetate, and oxaloacetate decarboxylases.
J. Am. Chem. Soc. 133(15) , 5683-5, (2011) To compare the powers of the corresponding enzymes as catalysts, the rates of uncatalyzed decarboxylation of several aliphatic acids (oxalate, malonate, acetoacetate, and oxaloacetate) were determined at elevated temperatures and extrapolated to 25 °C. In the... |
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Oxaloacetate decarboxylase of Archaeoglobus fulgidus: cloning of genes and expression in Escherichia coli.
Arch. Microbiol. 182(5) , 414-20, (2004) Archaeoglobus fulgidus harbors three consecutive and one distantly located gene with similarity to the oxaloacetate decarboxylase Na+ pump of Klebsiella pneumoniae (KpOadGAB). The water-soluble carboxyl transferase (AfOadA) and the biotin protein (AfOadC) wer... |
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Acid-inducible transcription of the operon encoding the citrate lyase complex of Lactococcus lactis Biovar diacetylactis CRL264.
J. Bacteriol. 186(17) , 5649-60, (2004) Although Lactococcus is one of the most extensively studied lactic acid bacteria and is the paradigm for biochemical studies of citrate metabolism, little information is available on the regulation of the citrate lyase complex. In order to fill this gap, we c... |
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A stable miniature protein with oxaloacetate decarboxylase activity.
ChemBioChem. 5(8) , 1075-80, (2004) An 18-residue miniature enzyme, Apoxaldie-1, has been designed, based on the known structure of the neurotoxic peptide apamin. Three lysine residues were introduced on the solvent-exposed face of the apamin alpha-helix to serve as an active site for decarboxy... |
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Characterization of an oxaloacetate decarboxylase that belongs to the malic enzyme family.
FEBS Lett. 570(1-3) , 217-22, (2004) The citM gene from Lactococcus lactis CRL264 was demonstrated to encode for an oxaloacetate decarboxylase. The enzyme exhibits high levels of similarity to malic enzymes (MEs) from other organisms. CitM was expressed in Escherichia coli, purified and its oxal... |
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Development of a markerless gene knock-out system for Mannheimia succiniciproducens using a temperature-sensitive plasmid.
FEMS Microbiol. Lett. 278(1) , 78-85, (2008) A temperature-sensitive derivative of the Mannheimia varigena plasmid pMVSCS1 was constructed by hydroxylamine treatment for use in the development of a markerless gene knock-out system for Mannheimia succiniciproducens. The temperature-sensitive plasmid pMVS... |
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Enzymatic assay for D-aspartic acid using D-aspartate oxidase and oxaloacetate decarboxylase.
Biosci. Biotechnol. Biochem. 76(11) , 2150-2, (2012) An enzymatic assay system for D-Asp was established using D-aspartate oxidase and oxaloacetate decarboxylase. In this system, D-Asp is converted to pyruvate, which is determined fluorometrically with 1,2-diamino-4,5-methylenedioxybenzene. This method makes po... |
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Crystal structures of Cg1458 reveal a catalytic lid domain and a common catalytic mechanism for the FAH family.
Biochem. J. 449(1) , 51-60, (2013) Cg1458 was recently characterized as a novel soluble oxaloacetate decarboxylase. However, sequence alignment identified that Cg1458 has no similarity with other oxaloacetate decarboxylases and instead belongs to the FAH (fumarylacetoacetate hydrolase) family.... |
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Identification of pyruvate carboxylase genes in Pseudomonas aeruginosa PAO1 and development of a P. aeruginosa-based overexpression system for alpha4- and alpha4beta4-type pyruvate carboxylases.
Appl. Environ. Microbiol. 72(12) , 7785-92, (2006) Pyruvate carboxylase (PYC) is an ecologically, medically, and industrially important enzyme. It is widespread in all three domains of life, the archaea, bacteria, and eukarya. PYC catalyzes ATP-dependent carboxylation of pyruvate to oxaloacetate. Detailed str... |