Title : Serine transhydroxymethylase. Equilibrium binding of folate analogs as active site probes.

Pub. Date : 1978 May 11

PMID : 656448






4 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 Formation of a quinoid-like structure within the glycyl-pyridoxal phosphate moiety of serine transhydroxymethylase (5,10-methylenetetrahydrofolate: glycine hydroxymethyltransferase, EC 2.1.2.1) is dependent upon the dissociation of the 2-S hydrogen of glycine which in turn requires the presence of tetrahydrofolate or analogs thereof. quinoid serine hydroxymethyltransferase 2 Homo sapiens
2 Formation of a quinoid-like structure within the glycyl-pyridoxal phosphate moiety of serine transhydroxymethylase (5,10-methylenetetrahydrofolate: glycine hydroxymethyltransferase, EC 2.1.2.1) is dependent upon the dissociation of the 2-S hydrogen of glycine which in turn requires the presence of tetrahydrofolate or analogs thereof. glycyl-pyridoxal phosphate serine hydroxymethyltransferase 2 Homo sapiens
3 Formation of a quinoid-like structure within the glycyl-pyridoxal phosphate moiety of serine transhydroxymethylase (5,10-methylenetetrahydrofolate: glycine hydroxymethyltransferase, EC 2.1.2.1) is dependent upon the dissociation of the 2-S hydrogen of glycine which in turn requires the presence of tetrahydrofolate or analogs thereof. Hydrogen serine hydroxymethyltransferase 2 Homo sapiens
4 Formation of a quinoid-like structure within the glycyl-pyridoxal phosphate moiety of serine transhydroxymethylase (5,10-methylenetetrahydrofolate: glycine hydroxymethyltransferase, EC 2.1.2.1) is dependent upon the dissociation of the 2-S hydrogen of glycine which in turn requires the presence of tetrahydrofolate or analogs thereof. 5,6,7,8-tetrahydrofolic acid serine hydroxymethyltransferase 2 Homo sapiens