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Literature summary for 2.1.2.1 extracted from

  • Talwar, R.; Leelavathy, V.; Rao, J.V.K.; Rao, N.A.; Savithri, H.S.
    Role of Pro-297 in the catalytic mechanism of sheep liver serine hydroxymethyltransferase (2000), Biochem. J., 350, 849-853.
No PubMed abstract available
Search for more literature for 2.1.2.1

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Ovis aries

Protein Variants

Protein Variants Comment Organism
P297R 85-90% loss of enzyme activity Ovis aries

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.9
-
 tetrahydrofolate
-
 Ovis aries
1
-
 L-serine
-
 Ovis aries
2.1
-
 tetrahydrofolate mutant enzyme Ovis aries
4
-
 L-serine mutant enzyme Ovis aries

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
210000
-
 wild-type and mutant enzyme, gelfiltation Ovis aries

Organism

Organism UniProt Comment Textmining
Ovis aries
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.6
-
 mutant enzyme Ovis aries
4.3
-
-
 Ovis aries

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-serine + tetrahydrofolate
-
 Ovis aries glycine + 5,10-methylenetetrahydrofolate + H2O
-
 ?
additional information enzyme catalyzes the pyridoxal 5'-phosphate dependent reversible cleavage of 3-hydroxy-alpha-amino acids Ovis aries ?
-
 ?

Subunits

Subunits Comment Organism
dimer removal of the bound pyridoxal 5'-phosphate from the mutant tetrameric enzyme leads to dissociation to a dimer Ovis aries
homotetramer
-
 Ovis aries

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
 Tm of wild-type and mutant enzyme: 54°C, in the presence of serine Tm of wild-type enzyme: 63°C Ovis aries
additional information
-
 L-serine increases the thermal stability Ovis aries

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.7
-
 L-serine mutant enzyme Ovis aries
4.2
-
 L-serine
-
 Ovis aries

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate one mol per subunit Ovis aries
pyridoxal 5'-phosphate important role in maintaining the structural integrity of the enzyme by preventing the dissociation of the enzyme into subunits, in addition to its function in catalysis Ovis aries