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asp-glu_1_decarboxylase |
Description |
Aspartate/Glutamate 1-decarboxylase (4.1.1.-) |
Catalyzed reaction |
L-aspartate = β-alanine + CO(2)
L-glutamate = 4-aminobutanoate + CO(2). |
Cofactor |
Pyridoxal-phosphate. |
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The recombinant protein from T. kodakaensis prefers L-Asp as its substrate rather than L-Glu, with nearly a 20-fold difference in catalytic efficiency.
In other enzymes, the two aminoacids react with similar efficiencies, or L-Glu is preferred.
In metazoa, L-Asp decarboxylation is carried out by Sulfinoalanine decarboxylase (4.1.1.29). |
Organisms |
-Archea |
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Family |
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Links |
Enzyme (activities) asp-glu_1_decarboxylase
BRENDA (activities) asp-glu_1_decarboxylase
KEGG (pathways) asp-glu_1_decarboxylase
PLPMDB (PLP mutants) asp-glu_1_decarboxylase
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References |
Tomita H, Yokooji Y, Ishibashi T, Imanaka T, Atomi H (2014) An archaeal glutamate decarboxylase homolog functions as an aspartate decarboxylase and is involved in β-alanine and CoA biosynthesis J Bacteriol 196 1222-30. Lee ES, Kim HW, Kim DE, Kim YH, Nam SW, Kim BW, Jeon SJ (2013) Gene expression and characterization of thermostable glutamate decarboxylase from Pyrococcus furiosus Biotechnol Bioproc Engin 18 375-381. Kim HW, Kashima Y, Ishikawa K, Yamano N (2009) Purification and characterization of the first archaeal glutamate decarboxylase from Pyrococcus horikoshii Biosci Biotechnol Biochem 73 224-7. Articles on asp-glu.1.decarboxylase |
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last changed |
2017/10/12 16:04 |
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