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

BRENDA support

Literature summary extracted from

  • Ohnishi, M.; Saito, M.; Wakabayashi, S.; Ishizuka, M.; Nishimura, K.; Nagata, Y.; Kasai, S.
    Purification and characterization of serine racemase from a hyperthermophylum Pyrobaculum islandicum (2007), J. Bacteriol., 190, 1359-1365.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.1.1.18 gene srr, DNA and amino acid sequence determination and anaylsis, expression in Escherichia coli Pyrobaculum islandicum

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.1.1.18 ATP 10-20% inhibition; 10-20% inhibition at 0.1-1 mM Pyrobaculum islandicum
5.1.1.18 Cu2+ 30-40% inhibition Pyrobaculum islandicum
5.1.1.18 Fe2+ 20-30% inhibition; 20-30% inhibition Pyrobaculum islandicum
5.1.1.18 hydroxylamine complete inhibition at 1 mM Pyrobaculum islandicum
5.1.1.18 additional information no inhibition by p-chloromercuribenzoate, iodoacetamide, and iodoacetate Pyrobaculum islandicum
5.1.1.18 Sodium borohydride complete inhibition at 1 mM Pyrobaculum islandicum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.1.1.18 additional information
-
 additional information the enzyme shows no allosteric properties, it is not affected by either L-isoleucine or L-valine, or most of the metal ions Pyrobaculum islandicum
5.1.1.18 additional information
-
 additional information enzyme shows no allosteric properties Pyrobaculum islandicum
5.1.1.18 95.4
-
 D-serine pH 8.2, 95°C Pyrobaculum islandicum
5.1.1.18 185
-
 L-serine pH 8.2, 95°C Pyrobaculum islandicum

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.1.1.18 Ca2+ activates Pyrobaculum islandicum
5.1.1.18 Cu2+ 30-40% stimulation Pyrobaculum islandicum
5.1.1.18 Mg2+ activates Pyrobaculum islandicum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.1.1.18 44000
-
 4 * 44000, native enzyme, SDS-PAGE Pyrobaculum islandicum
5.1.1.18 44000
-
 3 * 44000, SDS-PAGE Pyrobaculum islandicum
5.1.1.18 130000
-
 gel filtration Pyrobaculum islandicum
5.1.1.18 137000
-
 native enzyme, gel filtration Pyrobaculum islandicum
5.1.1.18 143000
-
 native enzyme, light scattering-refraction Pyrobaculum islandicum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.1.1.18 L-serine Pyrobaculum islandicum
-
 D-serine
-
 r
5.1.1.18 L-threonine Pyrobaculum islandicum
-
 D-threonine
-
 r

Organism

EC Number Organism UniProt Comment Textmining
5.1.1.18 Pyrobaculum islandicum
-
 bifunctional enzyme, shows additional L-serine/L-threonine dehydratase activity
-
5.1.1.18 Pyrobaculum islandicum Q2V0H1 anaerobic hyperthermophilic archaeon, strain DSM 4184, gene srr
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.1.1.18 native enzyme by anion exchange chromatography, recombinant enzyme from Escherichia coli by treatment with L-arginine and anion exchange chromatography Pyrobaculum islandicum

Source Tissue

EC Number Source Tissue Comment Organism Textmining
5.1.1.18 additional information optimal growth temperature of the organism is 100°C Pyrobaculum islandicum
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.1.1.18 13.6
-
 pH 8.2, 95°C Pyrobaculum islandicum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.1.18 D-serine 38% of the activity with L-serine Pyrobaculum islandicum L-serine
-
 r
5.1.1.18 D-threonine 13% of the activity with L-serine Pyrobaculum islandicum L-threonine
-
 r
5.1.1.18 L-serine
-
 Pyrobaculum islandicum D-serine
-
 r
5.1.1.18 L-serine the forward reaction is preferred, serine is preferred to threonine Pyrobaculum islandicum D-serine
-
 r
5.1.1.18 L-threonine
-
 Pyrobaculum islandicum D-threonine
-
 r
5.1.1.18 L-threonine the forward reaction is preferred, serine is preferred to threonine Pyrobaculum islandicum D-threonine
-
 r
5.1.1.18 L-threonine 40% of the activity with L-serine Pyrobaculum islandicum D-threonine
-
 r
5.1.1.18 additional information substrate specificity, the bifunctional enzyme shows high L-serine/L-threonine dehydratase activity, overview Pyrobaculum islandicum ?
-
 ?

Subunits

EC Number Subunits Comment Organism
5.1.1.18 tetramer 4 * 44000, native enzyme, SDS-PAGE Pyrobaculum islandicum
5.1.1.18 trimer 3 * 44000, SDS-PAGE Pyrobaculum islandicum

Synonyms

EC Number Synonyms Comment Organism
5.1.1.18 SRR
-
 Pyrobaculum islandicum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.1.1.18 95
-
-
 Pyrobaculum islandicum
5.1.1.18 95
-
 both racemase and dehydratase activity Pyrobaculum islandicum

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
5.1.1.18 50
-
 8 h, purified enzyme, 100 mM Tris-HCl buffer, pH 7.8, containing 0.01 mM pyridoxal 5’-phosphate, 95.2% remaining activity Pyrobaculum islandicum
5.1.1.18 75
-
 8 h, purified enzyme, 100 mM Tris-HCl buffer, pH 7.8, containing 0.01 mM pyridoxal 5’-phosphate, 67.1% remaining activity Pyrobaculum islandicum
5.1.1.18 95
-
 8 h, purified enzyme, 100 mM Tris-HCl buffer, pH 7.8, containing 0.01 mM pyridoxal 5’-phosphate, 29.8% remaining activity Pyrobaculum islandicum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.1.1.18 5.22
-
 D-serine pH 8.2, 95°C Pyrobaculum islandicum
5.1.1.18 14.8
-
 L-serine pH 8.2, 95°C Pyrobaculum islandicum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.1.1.18 8.2
-
-
 Pyrobaculum islandicum
5.1.1.18 8.2
-
 racemase activity Pyrobaculum islandicum

Cofactor

EC Number Cofactor Comment Organism Structure
5.1.1.18 pyridoxal 5'-phosphate
-
 Pyrobaculum islandicum
5.1.1.18 pyridoxal 5'-phosphate dependent on Pyrobaculum islandicum