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Literature summary extracted from

  • Jiang, W.; Chen, L.; Hu, N.; Yuan, S.; Li, B.; Liu, Z.
    A novel serine hydroxymethyltransferase from Arthrobacter nicotianae Characterization and improving catalytic efficiency by rational design (2015), BMC Biotechnol., 14, 93 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.1.2.1 EDTA 101.25% activity at 1% (v/v) Glutamicibacter nicotianae

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.2.1 expressed in Escherichia coli DE3 cells Glutamicibacter nicotianae

Protein Variants

EC Number Protein Variants Comment Organism
2.1.2.1 I249L the catalytic efficiency of the mutant is 2.78fold higher than that of the wild type enzyme Glutamicibacter nicotianae

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.2.1 CO(NH2)2 60.59% residual activity at 1 mM Glutamicibacter nicotianae
2.1.2.1 Co2+ 60.03% residual activity at 1 mM Glutamicibacter nicotianae
2.1.2.1 Cu2+ 8.95% residual activity at 1 mM Glutamicibacter nicotianae
2.1.2.1 dithiothreitol 59.29% residual activity at 1 mM Glutamicibacter nicotianae
2.1.2.1 Fe2+ complete inhibition at 1 mM Glutamicibacter nicotianae
2.1.2.1 Hg2+ complete inhibition at 1 mM Glutamicibacter nicotianae
2.1.2.1 Mn2+ 60.81% residual activity at 1 mM Glutamicibacter nicotianae
2.1.2.1 additional information the enzyme is not significantly influenced in activity by NH4+, Sl2+, Ca2+, Pb2+, SDS and CTAB Glutamicibacter nicotianae
2.1.2.1 Zn2+ 2.91% residual activity at 1 mM Glutamicibacter nicotianae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.2.1 57.86
-
 DL-3-phenylserine wild type enzyme, at pH 7.8 and 30°C Glutamicibacter nicotianae
2.1.2.1 61.95
-
 DL-3-phenylserine mutant enzyme I249L, at pH 7.8 and 30°C Glutamicibacter nicotianae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.1.2.1 Ba2+ 102.58% activity at 1 mM Glutamicibacter nicotianae
2.1.2.1 Mg2+ 108.38% activity at 1 mM Glutamicibacter nicotianae

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 Glutamicibacter nicotianae
-
 tetrahydrofolate + L-serine
-
 r
2.1.2.1 tetrahydrofolate + L-serine Glutamicibacter nicotianae
-
 5,10-methylenetetrahydrofolate + glycine + H2O
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.1.2.1 Glutamicibacter nicotianae U5TRK6
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.2.1 glutathione Sepharose column chromatography Glutamicibacter nicotianae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O
-
 Glutamicibacter nicotianae tetrahydrofolate + L-serine
-
 r
2.1.2.1 DL-3-phenylserine + ?
-
 Glutamicibacter nicotianae benzaldehyde + ?
-
 ?
2.1.2.1 tetrahydrofolate + L-serine
-
 Glutamicibacter nicotianae 5,10-methylenetetrahydrofolate + glycine + H2O
-
 r

Subunits

EC Number Subunits Comment Organism
2.1.2.1 ? x * 47300, calculated from amino acid sequence Glutamicibacter nicotianae

Synonyms

EC Number Synonyms Comment Organism
2.1.2.1 GlyA
-
 Glutamicibacter nicotianae
2.1.2.1 serine hydroxymethyltransferase
-
 Glutamicibacter nicotianae
2.1.2.1 SHMT
-
 Glutamicibacter nicotianae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.2.1 40
-
-
 Glutamicibacter nicotianae

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.1.2.1 30 65 the enzyme retains over 50% of the maximal activity at 30-65°C Glutamicibacter nicotianae

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.1.2.1 35 55 after 1 h incubation under pH 7.5, the enzyme retains over 35% of its maximal activity from 35°C to 45°C, but less than 15% at 55°C Glutamicibacter nicotianae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.1.2.1 1.6
-
 DL-3-phenylserine wild type enzyme, at pH 7.8 and 30°C Glutamicibacter nicotianae
2.1.2.1 4.8
-
 DL-3-phenylserine mutant enzyme I249L, at pH 7.8 and 30°C Glutamicibacter nicotianae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.2.1 7.5
-
-
 Glutamicibacter nicotianae

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.1.2.1 7 8 the enzyme shows more than 40% activity between pH 7.0 and 8.0. The enzyme displays less than 20% of its maximal activity at pH 5.5 and nearly no activity is detected below pH 2.5 Glutamicibacter nicotianae

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
2.1.2.1 5.5 8.5 the enzyme retains over 80% of the maximum activity over a pH range from 7.0 to 8.5 for 24 h at 4°C, and more than 70% of the maximal activity at pH 6.5. However, the enzyme exhibits a rapid decrease in activity at pH 5.5 Glutamicibacter nicotianae

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.2.1 pyridoxal 5'-phosphate
-
 Glutamicibacter nicotianae

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 0.028
-
 DL-3-phenylserine wild type enzyme, at pH 7.8 and 30°C Glutamicibacter nicotianae
2.1.2.1 0.077
-
 DL-3-phenylserine mutant enzyme I249L, at pH 7.8 and 30°C Glutamicibacter nicotianae