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4.1.1.29 |
Description |
Sulfinoalanine decarboxylase |
Alternative names |
Cysteine-sulfinate decarboxylase; Cysteine sulfinic acid decarboxylase; CSADCase. |
Catalyzed reaction |
3-sulfino-L-alanine = hypotaurine + CO(2). |
Cofactor |
Pyridoxal-phosphate. |
Comments |
-!- Also acts on l-cysteate. |
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The enzyme is involved in the biosynthesis of taurine, a sulfur-containing amino compound that apparently functions as a cytoprotectant and occurs at high concentration (5–50 mM) in most animal tissues.
The sequences of sulfinoalanine decarboxylases are strictly related to those of metazoan glutamate decarboxylases (4.1.1.15). |
PDB |
2JIS; |
Organisms |
-Metazoa -Human |
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Family |
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Links |
Enzyme (activities) 4.1.1.29
BRENDA (activities) 4.1.1.29
KEGG (pathways) 4.1.1.29
PLPMDB (PLP mutants) 4.1.1.29
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References |
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. Liu P, Ge X, Ding H, Jiang H, Christensen BM, Li J. (2012) Role of glutamate decarboxylase-like protein 1 (GADL1) in taurine biosynthesis. J Biol Chem. 287 40898-906. Park, E.; Park, S.Y.; Wang, C.; Xu, J.; LaFauci, G.; Schuller-Levis, G. (2002) Cloning of murine cysteine sulfinic acid decarboxylase and its mRNA expression in murine tissues Biochim Biophys Acta 1574 403-06. Tappaz, M.; Bitoun, M.; Reymond, I.; Sergeant, A. (1999) Characterization of the cDNA coding for rat brain cysteine sulfinate decarboxylase: brain and liver enzymes are identical proteins encoded by two distinct mRNAs J Neurochem 73 903-12. Reymond I, Sergeant A, Tappaz M. (1996) Molecular cloning and sequence analysis of the cDNA encoding rat liver cysteine sulfinate decarboxylase (CSD) Biochim Biophys Acta 1307 152-6. Articles on 4.1.1.29 |
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last changed |
2019/03/26 11:56 |
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