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Literature summary for 2.1.2.1 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
Search for more literature for 2.1.2.1

Activating Compound

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

Cloned(Commentary)

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

Protein Variants

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

Inhibitors

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

KM Value [mM]

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5,10-methylenetetrahydrofolate + glycine + H2O Glutamicibacter nicotianae
-
 tetrahydrofolate + L-serine
-
 r
tetrahydrofolate + L-serine Glutamicibacter nicotianae
-
 5,10-methylenetetrahydrofolate + glycine + H2O
-
 r

Organism

Organism UniProt Comment Textmining
Glutamicibacter nicotianae U5TRK6
-
-

Purification (Commentary)

Purification (Comment) Organism
glutathione Sepharose column chromatography Glutamicibacter nicotianae

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
GlyA
-
 Glutamicibacter nicotianae
serine hydroxymethyltransferase
-
 Glutamicibacter nicotianae
SHMT
-
 Glutamicibacter nicotianae

Temperature Optimum [°C]

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

Temperature Range [°C]

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
 Glutamicibacter nicotianae

pH Range

pH Minimum pH Maximum Comment Organism
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

pH Stability pH Stability Maximum Comment Organism
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

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Glutamicibacter nicotianae

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.028
-
 DL-3-phenylserine wild type enzyme, at pH 7.8 and 30°C Glutamicibacter nicotianae
0.077
-
 DL-3-phenylserine mutant enzyme I249L, at pH 7.8 and 30°C Glutamicibacter nicotianae