Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.1.2.1 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)

Crystallization (Comment) Organism
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

Protein Variants Comment Organism
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
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

Organism UniProt Comment Textmining
Geobacillus stearothermophilus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Geobacillus stearothermophilus

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
SHMT
-
Geobacillus stearothermophilus

Cofactor

Cofactor Comment Organism Structure
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