Reactome | SHMT1 tetramer cleaves HTMLYS to yield TEABL and Gly

SHMT1 tetramer cleaves HTMLYS to yield TEABL and Gly

Stable Identifier

R-HSA-71249

Type

Reaction [transition]

Species

Homo sapiens

Compartment

cytosol

Synonyms

(3S)-3-hydroxy-N(6),N(6),N(6)-trimethyl-L-lysine => 4-(trimethylamino)butanal + glycine, beta-hydroxy-trimethyllysine => gamma-butyrobetaine aldehyde + glycine

ReviewStatus

5/5

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SHMT1 tetramer cleaves HTMLYS to yield TEABL and Gly

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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) purified a tetrameric cytosolic rat 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. Vaz & Wanders (2002) inferred that this enzyme and its human ortholog mediate the cleavage of HTMLYS to yield TEABL and Gly in vivo. This inference has been confirmed by computational docking studies and assays of the activity of purified recombinant human enzyme in vitro (Percudani et al. 2023).

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
	One substrate - many enzymes virtual screening uncovers missing genes of carnitine biosynthesis in human and mouse (preprint) Malatesta, M, Polverini, E, Di Salvo, M, Battistutta, R, Peracchi, A, Percudani, R, Tramonti, A, Gabriele, G, Contestabile, R, Fornasier, R, Secchi, A, Zangelmi, E
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