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Literature summary for 5.4.2.7 extracted from

  • Leer, J.C.; Hammer-Jespersen, K.
    Multiple forms of phosphodeoxyribomutase from Escherichia coli. Physical and chemical characterization (1975), Biochemistry, 14, 599-607.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
ribose-1,5-diphosphate stimulates, Km: 0.00024 mM for enzyme form I, 0.00027 mM for enzyme form II and 0.00029 mM for enzyme form III Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.014
-
deoxyribose 1-phosphate enzyme form I Escherichia coli
0.015
-
deoxyribose 1-phosphate enzyme form II Escherichia coli
0.022
-
deoxyribose 1-phosphate enzyme form III Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
45000
-
equilibrium centrifugation Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
multiple forms: I, II, II-1 and III-2 Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
142
-
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-ribose 1-phosphate
-
Escherichia coli D-ribose 5-phosphate
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
25
-
half-life of the cobalt-enzyme in 1 mM EDTA: 15 min for enzyme form I, 31 min for enzyme form II Escherichia coli