PXLP-K333-GADL1 decarboxylates acidic AAs

Stable Identifier
R-HSA-6787757
Type
Reaction
Species
Homo sapiens
Compartment
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Acidic amino acid decarboxylase GADL1 (GADL1) can decarboxylate aspartate, cysteine sulfinic acid, and cysteic acid to beta-alanine, hypotaurine and taurine, respectively but does not exhibit any decarboxylation activity toward glutamate (Liu et al. 2012, 2013). The dimeric structure of the enzyme is inferred from studies of its mouse homolog (Raasakka et al. 2018).

Literature References
PubMed ID Title Journal Year
23038267 Role of glutamate decarboxylase-like protein 1 (GADL1) in taurine biosynthesis

Christensen, BM, Li, J, Ge, X, Ding, H, Jiang, H, Liu, P

J. Biol. Chem. 2012
22718265 Mechanism of cysteine-dependent inactivation of aspartate/glutamate/cysteine sulfinic acid α-decarboxylases

Torrens-Spence, MP, Christensen, BM, Li, J, Ding, H, Liu, P

Amino Acids 2013
29372909 Structure of the mouse acidic amino acid decarboxylase GADL1

Haavik, J, Kursula, P, Luan, W, Raasakka, A, Winge, I, Mahootchi, E

Acta Crystallogr F Struct Biol Commun 2018
Participants
Participates
Catalyst Activity

carboxy-lyase activity of PXLP-K333-GADL1 dimer [cytosol]

Orthologous Events
Cross References
Rhea
Authored
Reviewed
Created
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