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4.1.1.11 |
Description |
Aspartate 1-decarboxylase |
Alternative names |
Aspartate-1-decarboxylase;
Cysteine sulfinate decarboxylase. |
Catalyzed reaction |
L-aspartate = beta-alanine + CO(2). |
Cofactor |
Pyridoxal-phosphate or pyruvate. |
Comments |
The Escherichia coli enzyme contains a pyruvoyl group. |
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The same activity is carried out by PLP-dependent enzymes in some organisms, such as insects (where the corresponding enzymes also have cysteine sulfinate decarboxylase activity, and have been included in family 4.1.1.29) or Methanocaldococcus jannaschii (activity is carried out by a tyrosine aminotransferase, see family 4.1.1.25 b).
Other archaeal enzymes acting on both Aspartate and Glutamate have been included in family asp-glu_1_decarboxylase. |
Organisms |
-Archea -Metazoa |
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Family |
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Links |
Enzyme (activities) 4.1.1.11
BRENDA (activities) 4.1.1.11
KEGG (pathways) 4.1.1.11
PLPMDB (PLP mutants) 4.1.1.11
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References |
Pan S, Nikolakakis K, Adamczyk PA, Pan M, Ruby EG, Reed JL (2017) Model-enabled gene search (MEGS) allows fast and direct discovery of enzymatic and transport gene functions in the marine bacterium Vibrio fischeri J Biol Chem 292 10250-10261. Wang Y, Xu H, White RH (2014) β-alanine biosynthesis in Methanocaldococcus jannaschii J Bacteriol 196 2869-75. Liu P, Ding H, Christensen BM, Li J. (2012) Cysteine sulfinic acid decarboxylase activity of Aedes aegypti aspartate 1-decarboxylase: the structural basis of its substrate selectivity. Insect Biochem Mol Biol. 42 396-403. Articles on 4.1.1.11 |
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last changed |
2018/05/07 14:00 |
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