SDS dimers:PXLP convert L-Ser to PYR and NH4+

Stable Identifier
R-HSA-9929460
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Synonyms
L-serine => NH4(+) + pyruvate
ReviewStatus
5/5
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Both SDS (L-serine dehydratase/L-threonine deaminase) and SDSL (Serine dehydratase-like), covalently conjugated with PXLP, form dimers that catalyze the reaction of L-serine (L-Ser) to form pyruvate (PYR) and ammonium (NH4+). These reactions occur in the cytosol (Ogawa et al. 2006; Yamada et al. 2008).
Literature References
PubMed ID Title Journal Year
18342636 A catalytic mechanism that explains a low catalytic activity of serine dehydratase like-1 from human cancer cells: crystal structure and site-directed mutagenesis studies

Yamada, T, Komoto, J, Kasuya, T, Takata, Y, Ogawa, H, Mori, H, Takusagawa, F

Biochim. Biophys. Acta 2008
16580895 Enzymatic and biochemical properties of a novel human serine dehydratase isoform

Ogawa, H, Gomi, T, Nishizawa, M, Hayakawa, Y, Endo, S, Hayashi, K, Ochiai, H, Takusagawa, F, Pitot, HC, Mori, H, Sakurai, H, Koizumi, K, Saiki, I, Oda, H, Fujishita, T, Miwa, T, Maruyama, M, Kobayashi, M

Biochim Biophys Acta 2006
Participants
Participates
Catalyst Activity

L-serine ammonia-lyase activity of PXLP-SDS dimers [cytosol]

Orthologous Events
Cross References
RHEA
Authored
Reviewed
Created
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