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Literature summary extracted from

  • Bhavani, S.; Trivedi, V.; Jala, V.R.; Subramanya, H.S.; Kaul, P.; Prakash, V.; Appaji Rao, N.; Savithri, H.S.
    Role of Lys-226 in the catalytic mechanism of Bacillus stearothermophilus serine hydroxymethyltransferase--crystal structure and kinetic studies (2005), Biochemistry, 44, 6929-6937.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.2.1 crystals of K226M and K226Q mutant enzymes and of the complex of mutant enzyme K226Q with Gly or mutant enzyme K226M with Ser. Crystals are obtained by mixing 0.004 ml of protein solution 0.375 mM with 0.004 mM of reservoir solution containing 100 mM Hepes buffer, pH 7.5, 0.2 mM EDTA, 5 mM 2-mercaptoethanol, and 50% 2-methyl-2,4-pentanediol Geobacillus stearothermophilus

Protein Variants

EC Number Protein Variants Comment Organism
2.1.2.1 K226M mutant enzymes is inactive, drastic rate of formation of the quinoid intermediate. It contains 1 mol of pyridoxal 5'-phosphate per mol of subunit. pyridoxal 5'-phosphate is bound at the active site in an orientation different from that of the wild-type enzyme. K-226 is responsible for flipping of pyridoxal 5'-phosphate from one orientation to another which is crucial for tetrahydropteroylglutamate-dependent Calpha-Cbeta bond cleavage of L-Ser Geobacillus stearothermophilus
2.1.2.1 K226Q mutant enzymes is inactive, drastic rate of formation of the quinoid intermediate. It contains 1 mol of pyridoxal 5'-phosphate oer mol of subunit. pyridoxal 5'-phosphate is bound at the active site in an orientation different from that of the wild-type enzyme. K-226 is responsible for flipping of pyridoxal 5'-phosphate from one orientation to another which is crucial for tetrahydropteroylglutamate-dependent Calpha-Cbeta bond cleavage of L-Ser Geobacillus stearothermophilus

Organism

EC Number Organism UniProt Comment Textmining
2.1.2.1 Geobacillus stearothermophilus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.2.1
-
 Geobacillus stearothermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.2.1 L-Ser + tetrahydrofolate
-
 Geobacillus stearothermophilus Gly + 5,10-methylenetetrahydrofolate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.2.1 SHMT
-
 Geobacillus stearothermophilus

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.2.1 pyridoxal 5'-phosphate mutant enzymes K226M and K226Q contain 1 mol of pyridoxal 5'-phosphate per mol of subunit. Pyridoxal 5'-phosphate is bound at the active site in an orientation different from that of the wild-type enzyme. K226 is responsible for flipping of pyridoxal 5'-phosphate from one orientation to another which is crucial for tetrahydropteroylglutamate-dependent Calpha-Cbeta bond cleavage of L-Ser Geobacillus stearothermophilus