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Literature summary for 2.4.2.10 extracted from

  • Shimosaka, M.; Fukuda, Y.; Murata, K.; Kimura, A.
    Purification and properties of orotate phosphoribosyltransferases from Escherichia coli K-12, and its derivative purine-sensitive mutant (1985), J. Biochem., 98, 1689-1697.
    View publication on PubMed
Search for more literature for 2.4.2.10

Inhibitors

Inhibitors Comment Organism Structure
adenine not inhibitory Escherichia coli
adenosine not inhibitory Escherichia coli
ADP not inhibitory Escherichia coli
AMP not inhibitory Escherichia coli
ATP not inhibitory Escherichia coli
HgCl2 slight inhibition of mutant, not wild-type Escherichia coli
iodoacetamide slight inhibition of mutant, not wild-type Escherichia coli
NEM slight inhibition of mutant, not wild-type Escherichia coli
PCMB reversible by DTT Escherichia coli
UTP not inhibitory Escherichia coli
Zn2+
-
 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0031 0.0036 orotidine 5'-phosphate wild-type Escherichia coli
0.013
-
 diphosphate wild-type Escherichia coli
0.03
-
 orotidine 5'-monophosphate
-
 Escherichia coli
0.03 0.035 Orotate wild-type Escherichia coli
0.038 0.04 5-phospho-alpha-D-ribose 1-diphosphate wild-type Escherichia coli
0.22 0.25 diphosphate
-
 Escherichia coli
0.36
-
 5-phospho-alpha-D-ribose 1-diphosphate mutant Escherichia coli
0.44
-
 Orotate mutant Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Ba2+ slight activation Escherichia coli
Ca2+ activation, 34% as effective as Mn2+ or Mg2+ Escherichia coli
Co2+ slight activation Escherichia coli
Mg2+ requirement Escherichia coli
Mn2+ can replace Mg2+ Escherichia coli
Mn2+ activation Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
23500
-
 2 * 23500, SDS-PAGE Escherichia coli
47000
-
 K-12, gel filtration Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
orotate + 5-phospho-alpha-D-ribose 1-diphosphate Escherichia coli involved in de novo synthesis of pyrimidine nucleotides orotidine 5'-phosphate + diphosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 K-12, overproducing strains C-600(pNE24) (wild-type) and its purine-sensitive mutant PS100(pNE31), both harbouring hybrid multi-copy plasmids
-

Purification (Commentary)

Purification (Comment) Organism
OMP-agarose affinity chromatography Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Escherichia coli
0.41
-
 mutant Escherichia coli
15.2
-
 wild-type Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
orotate + 5-phospho-alpha-D-ribose 1-diphosphate reverse reaction: tri-, tetrapoly- or trimetaphosphate can replace diphosphate with 29%, 70% or 78% efficiency Escherichia coli orotidine 5'-phosphate + diphosphate
-
 r
orotate + 5-phospho-alpha-D-ribose 1-diphosphate involved in de novo synthesis of pyrimidine nucleotides Escherichia coli orotidine 5'-phosphate + diphosphate
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 23500, SDS-PAGE Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
 mutant Escherichia coli
9.5
-
 wild-type Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
7.2 9.5 about half-maximal activity at pH 7.2 and 9.5, mutant Escherichia coli
8.5 10.5 about half-maximal activity at pH 8.5 and about 70% of maximal activity at pH 10.5, wild-type Escherichia coli