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Literature summary extracted from

  • Haque, M.; Hirowatari, A.; Nai, N.; Furuya, S.; Yamamoto, K.
    Serine hydroxymethyltransferase from the silkworm Bombyx mori Identification, distribution, and biochemical characterization (2019), Arch. Insect Biochem. Physiol., 102, e21594 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.2.1 expressed in Escherichia coli BL21(DE3) cells Bombyx mori

Protein Variants

EC Number Protein Variants Comment Organism
2.1.2.1 H119A the mutant shows reduced activity compared to the wild type enzyme Bombyx mori
2.1.2.1 H132A the mutant shows reduced activity compared to the wild type enzyme Bombyx mori
2.1.2.1 H135A the mutant shows reduced activity compared to the wild type enzyme Bombyx mori

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.2.1 0.003
-
tetrahydrofolate mutant enzyme H135A, in the presence of NADP+, at pH 3.0 and 30°C Bombyx mori
2.1.2.1 0.0031
-
tetrahydrofolate mutant enzyme H119A, in the presence of NADP+, at pH 3.0 and 30°C Bombyx mori
2.1.2.1 0.014
-
tetrahydrofolate mutant enzyme H132A, in the presence of NADP+, at pH 3.0 and 30°C Bombyx mori
2.1.2.1 0.055
-
tetrahydrofolate wild type enzyme, in the presence of NADP+, at pH 3.0 and 30°C Bombyx mori
2.1.2.1 1.8
-
L-serine wild type enzyme, in the presence of NADP+, at pH 3.0 and 30°C Bombyx mori
2.1.2.1 3.3
-
L-serine mutant enzyme H135A, in the presence of NADP+, at pH 3.0 and 30°C Bombyx mori
2.1.2.1 4.2
-
L-serine mutant enzyme H119A, in the presence of NADP+, at pH 3.0 and 30°C Bombyx mori

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 Bombyx mori
-
tetrahydrofolate + L-serine
-
r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O Bombyx mori p50T
-
tetrahydrofolate + L-serine
-
r
2.1.2.1 tetrahydrofolate + L-serine Bombyx mori
-
5,10-methylenetetrahydrofolate + glycine + H2O
-
r
2.1.2.1 tetrahydrofolate + L-serine Bombyx mori p50T
-
5,10-methylenetetrahydrofolate + glycine + H2O
-
r

Organism

EC Number Organism UniProt Comment Textmining
2.1.2.1 Bombyx mori
-
-
-
2.1.2.1 Bombyx mori p50T
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.2.1 Ni2+-affinity column chromatography and Superdex S200 gel filtration Bombyx mori

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.1.2.1 fat body
-
Bombyx mori
-
2.1.2.1 hemocyte
-
Bombyx mori
-
2.1.2.1 larva
-
Bombyx mori
-
2.1.2.1 midgut
-
Bombyx mori
-
2.1.2.1 ovary highest expression Bombyx mori
-
2.1.2.1 silk gland
-
Bombyx mori
-
2.1.2.1 testis high expression Bombyx mori
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O
-
Bombyx mori tetrahydrofolate + L-serine
-
r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O
-
Bombyx mori p50T tetrahydrofolate + L-serine
-
r
2.1.2.1 tetrahydrofolate + L-serine
-
Bombyx mori 5,10-methylenetetrahydrofolate + glycine + H2O
-
r
2.1.2.1 tetrahydrofolate + L-serine
-
Bombyx mori p50T 5,10-methylenetetrahydrofolate + glycine + H2O
-
r

Subunits

EC Number Subunits Comment Organism
2.1.2.1 ? x * 50000, SDS-PAGE Bombyx mori

Synonyms

EC Number Synonyms Comment Organism
2.1.2.1 serine hydroxymethyltransferase
-
Bombyx mori
2.1.2.1 SHMT
-
Bombyx mori

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.2.1 30
-
-
Bombyx mori

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.1.2.1 25 35 the enzyme shows about 35% activity at 25 or 35°C Bombyx mori

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.1.2.1 20 40 the enzyme retains more than 80% of its activity after 30 min at 20-40°C. After 30 min at 45-50°C, the enzyme shows about 30% residual activity. The enzyme shows about 30% activity after 30 min at pH 10-12 Bombyx mori

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.2.1 3
-
-
Bombyx mori

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.1.2.1 2 4 about 60% activity at pH 2.0, 100% activity at pH 3.0, about 20% activity at pH 4.0 Bombyx mori

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
2.1.2.1 2 7 the enzyme retains more than 50% of its activity after 30 min at pH 2.0-7.0 Bombyx mori

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.2.1 pyridoxal 5'-phosphate
-
Bombyx mori

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.1.2.1 0.00065
-
L-serine mutant enzyme H119A, in the presence of NADP+, at pH 3.0 and 30°C Bombyx mori
2.1.2.1 0.00071
-
L-serine mutant enzyme H135A, in the presence of NADP+, at pH 3.0 and 30°C Bombyx mori
2.1.2.1 0.0022
-
L-serine wild type enzyme, in the presence of NADP+, at pH 3.0 and 30°C Bombyx mori
2.1.2.1 0.011
-
tetrahydrofolate mutant enzyme H132A, in the presence of NADP+, at pH 3.0 and 30°C Bombyx mori
2.1.2.1 0.047
-
tetrahydrofolate mutant enzyme H135A, in the presence of NADP+, at pH 3.0 and 30°C Bombyx mori
2.1.2.1 0.074
-
tetrahydrofolate mutant enzyme H119A, in the presence of NADP+, at pH 3.0 and 30°C Bombyx mori
2.1.2.1 0.081
-
tetrahydrofolate wild type enzyme, in the presence of NADP+, at pH 3.0 and 30°C Bombyx mori