The human cytosolic serine hydroxymethyltransferase /Deltaflap variant exhibited different catalytic properties in (6S)-tetrahydrofolate (THF)-dependent reactions compared with the WT but had similar activity in THF-independent aldol cleavage of beta-hydroxyamino acid.
Characterized the serine hydroxymethyltransferase reaction catalyzed by SHMT1 and SHMT2 with a focus on pH dependence and substrate inhibition. SHMT2 maintains a pronounced tetrahydrofolate substrate inhibition even at the alkaline pH characteristic of the mitochondrial matrix whereas with SHMT1 this is almost abolished. At this pH SHMT2 also shows a catalytic efficiency that is much higher than that of SHMT1.
genotypes TT (SHMT1 rs4925166) CC (ERG rs2836425) GG (MAZ rs34286592) and GG (SHMT1 rs1979277) had the highest negative association (protective effect) with multiple sclerosis
Studied association of essential hypertension (EH) predisposition and methylation patterns in promoter region of serine hydroxymethyltransferase 1(SHMT1); found SHMT1 promoter hypermethylation increases risk of EH and is a possible biomarker for EH.
Methylene tetrahydrofolate reductase (MTHFR) C677T 5-methyltetrahydrofolate homocysteine methyltransferase (MTR) A2756G and 5- methyltetrahydrofolate homocysteine methyltransferase reductase (MTRR) A66G were shown to be positively associatiated with homocysteine while nonvegetarian diet serine hydroxymethyltransferase 1 (SHMT1) C1420T and TYMS 5'-UTR 28 bp tandem repeat exhibited negative association with homocysteine.
The one-carbon donor formate generally rescues cells from SHMT inhibition but paradoxically increases the inhibitor's cytotoxicity in diffuse large B-cell lymphoma (DLBCL); this effect is rooted in defective glycine uptake in DLBCL cell lines rendering them uniquely dependent upon SHMT enzymatic activity to meet glycine demand.
The present study using both case-control and family-based triad approach is the first report to demonstrate parental association of SHMT1 C1420T variant in conferring NTD risk in the fetus.
SHMT1 controls the expression of pro-oncogenic inflammatory cytokines by regulating sialic acid Neu5Ac to promote ovarian cancer tumor growth and migration.
Site-directed mutagenesis experiments on SHMT1 demonstrate that selective enzyme inhibition relies on the presence of a cysteine residue at the active site of SHMT1 (Cys204) that is absent in SHMT2.
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