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Literature summary extracted from

  • Schweitzer, J.E.; Stolz, M.; Diesveld, R.; Etterich, H.; Eggeling, L.
    The serine hydroxymethyltransferase gene glyA in Corynebacterium glutamicum is controlled by GlyR (2009), J. Biotechnol., 139, 214-221.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
2.1.2.1 Corynebacterium glutamicum
-
 strain ATCC13032
-
2.1.2.1 Corynebacterium glutamicum ATCC 13032
-
 strain ATCC13032
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.1.2.1 0.0385
-
 in the presence of glycine, in 200 mM HEPES buffer, pH 7.0 Corynebacterium glutamicum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.2.1 L-serine + tetrahydrofolate
-
 Corynebacterium glutamicum glycine + 5,10-methylenetetrahydrofolate + H2O
-
 ?
2.1.2.1 L-serine + tetrahydrofolate
-
 Corynebacterium glutamicum ATCC 13032 glycine + 5,10-methylenetetrahydrofolate + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.2.1 serine hydroxymethyltransferase
-
 Corynebacterium glutamicum
2.1.2.1 SHMT
-
 Corynebacterium glutamicum

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.2.1 pyridoxal 5'-phosphate
-
 Corynebacterium glutamicum

Expression

EC Number Organism Comment Expression
2.1.2.1 Corynebacterium glutamicum about 3fold increase of SHMT activity during exponential growth with a further increase at the onset of the stationary phase, the essential SHMT has highest activity in the stationary phase and the regulator GlyR acts as an activator of transcription in this growth phase. Addition of glycine results in a slight but significant increase of SHMTactivity by 75% up