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Literature summary extracted from

  • Kandoth, P.K.; Liu, S.; Prenger, E.; Ludwig, A.; Lakhssassi, N.; Heinz, R.; Zhou, Z.; Howland, A.; Gunther, J.; Eidson, S.; Dhroso, A.; LaFayette, P.; Tucker, D.; Johnson, S.; Anderson, J.; Alaswad, A.; Cianzio, S.R.; Parrott, W.A.; Korkin, D.; Meksem, K.; Mitchum, M.G.
    Systematic mutagenesis of serine hydroxymethyltransferase reveals an essential role in nematode resistance (2017), Plant Physiol., 175, 1370-1380 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.2.1 expressed in Escherichia coli GS245(DE3)pLysS cells Glycine max

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O Glycine max
-
tetrahydrofolate + L-serine
-
r
2.1.2.1 tetrahydrofolate + L-serine Glycine max
-
5,10-methylenetetrahydrofolate + glycine + H2O
-
r

Organism

EC Number Organism UniProt Comment Textmining
2.1.2.1 Glycine max
-
cultivar Williams 82
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O
-
Glycine max tetrahydrofolate + L-serine
-
r
2.1.2.1 tetrahydrofolate + L-serine
-
Glycine max 5,10-methylenetetrahydrofolate + glycine + H2O
-
r

Synonyms

EC Number Synonyms Comment Organism
2.1.2.1 Rhg4
-
Glycine max
2.1.2.1 serine hydroxymethyltransferase
-
Glycine max
2.1.2.1 SHMT08
-
Glycine max

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.2.1 pyridoxal 5'-phosphate
-
Glycine max

General Information

EC Number General Information Comment Organism
2.1.2.1 physiological function the enzyme has additional functions aside from its main enzymatic role in soybean cyst nematode resistance Glycine max