SHMT1 tetramer cleaves HTMLYS to yield TEABL and Gly

Stable Identifier
Reaction [transition]
Homo sapiens
beta-hydroxy-trimethyllysine => gamma-butyrobetaine aldehyde + glycine
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Cytosolic serine hydroxymethyltransferase tetramer (SHMT1) catalyzes the reaction of (3S)-3-hydroxy-N(6),N(6),N(6)-trimethyl-L-lysine(1+) (NTMLYS) to form glycine (Gly) and 4-trimethylammoniobutanal (TEABL). Ogata & Fujioka (1981) and Masuda et al. (1987) have each purified to apparent homogeneity a cytosolic enzyme that in the presence of tetrahydrofolate catalyzes the conversion of serine to glycine but that in its absence catalyzes the cleavage of L-allothreonine to glycine and an aldehyde. The native enzyme appears to be a tetramer. This rat enzyme and its human ortholog are inferred to mediate the cleavage of HTMLYS to yield TEABL and Gly in vivo (Vaz & Wanders 2002).

Literature References
PubMed ID Title Journal Year
3110140 Affinity purification and characterization of serine hydroxymethyltransferases from rat liver

Hayashi, H, Sakamoto, M, Wada, H, Yamamoto, M, Nishizaki, I, Masuda, T

J Biochem 1987
11802770 Carnitine biosynthesis in mammals

Vaz, FM, Wanders, RJA

Biochem J 2002
6795186 Purification and characterization of cytosolic and mitochondrial serine hydroxymethyltransferases from rat liver

Ogawa, H, Fujioka, M

J Biochem 1981
Catalyst Activity

aldehyde-lyase activity of SHMT1 tetramer [cytosol]

Orthologous Events
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