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4.1.1.29 |
Activity |
4.1.1.29 |
Description |
Sulfinoalanine decarboxylase |
Notes |
The mammalian sequences in this family are strictly related to those of metazoan glutamate decarboxylases (4.1.1.15_a). The insect enzymes (e.g., the one from Aedes egypti) also possess a substantial aspartate 1-decarboxylase activity and are often annotated as Aspartate 1-decarboxylases. |
PDB |
2JIS; |
PLP Fold Type |
I |
PLP-dependent Domain |
|
Number of sequences |
11 |
Sequences in seed alignment |
|
Reference sequence |
CSD_HUMAN |
Domain interval |
49-417 |
Catalytic site |
305 K |
| |
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. 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 |
last changed |
2018/05/07 13:37 |
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