Skip to search formSkip to main content
You are currently offline. Some features of the site may not work correctly.

oxaloacetate decarboxylase activity

Known as: oxalacetic acid decarboxylase activity, oxaloacetate beta-decarboxylase activity, oxaloacetate carboxy-lyase (pyruvate-forming) 
Catalysis of the reaction: oxaloacetate = pyruvate + CO2. [EC:1.1.1.38, EC:1.1.1.40, EC:4.1.1.3]
National Institutes of Health

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Review
2014
Review
2014
Functionally diverse biotin-dependent enzymes with oxaloacetate decarboxylase activity.
Biotin-dependent enzymes catalyze carboxylation, decarboxylation and transcarboxylation reactions that participate in the primary… Expand
  • figure 1
  • figure 2
  • figure 4
  • figure 5
  • figure 6
2004
2004
A Stable Miniature Protein with Oxaloacetate Decarboxylase Activity
An 18‐residue miniature enzyme, Apoxaldie‐1, has been designed, based on the known structure of the neurotoxic peptide apamin… Expand
2001
2001
Design, synthesis and characterisation of a peptide with oxaloacetate decarboxylase activity.
The synthesis of Oxaldie-3, a synthetic 31-residue peptide with oxaloacetate decarboxylase activity, is described. Biophysical… Expand
2001
2001
Mutation Arg336 to Lys in Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase originates an enzyme with increased oxaloacetate decarboxylase activity
Saccharomyces cerevisiae phosphoenolpyruvate (PEP) carboxykinase catalyzes one of the first reactions in the biosynthesis of… Expand
1998
1998
The strongly conserved lysine 256 of Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase is essential for phosphoryl transfer.
Lysine 256, a conserved amino acid of Saccharomycescerevisiae phosphoenolpyruvate (PEP) carboxykinase located in the consensus… Expand
1995
1995
A mutant phosphoenolpyruvate carboxykinase in Escherichia coli conferring oxaloacetate decarboxylase activity.
The phosphoenolpyruvate carboxykinase in Escherichia coli (encoded by pck) catalyzes the conversion from oxaloacetate (OAA) to… Expand
  • figure 1
  • figure 2
  • table 1
  • figure 4
  • figure 3
1991
1991
Chemical modification of Pseudomonas ochraceae 4-hydroxy-4-methyl-2-oxoglutarate aldolase by diethyl pyrocarbonate.
  • K. Maruyama
  • Journal of biochemistry
  • 1991
    • Corpus ID: 32366465
Diethyl pyrocarbonate inactivates Pseudomonas ochraceae 4-hydroxy-4-methyl-2-oxoglutarate aldolase [4-hydroxy-4-methyl-2… Expand
1990
1990
Purification and properties of 4-hydroxy-4-methyl-2-oxoglutarate aldolase from Pseudomonas ochraceae grown on phthalate.
  • K. Maruyama
  • Journal of biochemistry
  • 1990
    • Corpus ID: 23947248
4-Hydroxy-4-methyl-2-oxoglutarate aldolase [4-hydroxy-4-methyl-2-oxoglutarate pyruvate-lyase: EC 4.1.3.17] has been purified to… Expand
1988
1988
Oxalacetate decarboxylase and pyruvate carboxylase activities, and effect of sulfhydryl reagents in malic enzyme from Sulfolobus solfataricus.
Malic enzyme (S)-malate: NADP+ oxidoreductase (oxaloacetate-decarboxylating, EC 1.1.1.40) purified from the thermoacidophilic… Expand
1987
1987
Isolation, properties and role in progesterone biosynthesis of cytosolic malic enzyme from human term placenta.
Cytosolic malic enzyme (L-malate: NADP oxidoreductase decarboxylating, EC I. I. I.40) has been isolated and purified from… Expand
By clicking accept or continuing to use the site, you agree to the terms outlined in our Privacy Policy, Terms of Service, and Dataset License
ACCEPT & CONTINUE