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Literature summary for 2.7.1.175 extracted from

  • Jarling, M.; Cauvet, T.; Grundmeier, M.; Kuhnert, K.; Pape, H.
    Isolation of mak1 from Actinoplanes missouriensis and evidence that Pep2 from Streptomyces coelicolor is a maltokinase (2004), J. Basic Microbiol., 44, 360-373.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene mak1, located in a gene cluster, DNA and amino acid sequence determination and analysis, sequence comparisons, expression of the His-tagged enzyme in Streptomyces lividans strain 66 using vector pMJP7 Actinoplanes missouriensis
gene pep2, sequence comparisons, expression of the His-tagged enzyme in Streptomyces lividans strain 66 using vector pMJP7 Streptomyces coelicolor

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Streptomyces coelicolor

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
49800
-
x * 49800, His-tagged enzyme, sequence calculation, x * 62000, recombinant His-tagged enzyme, SDS-PAGE Actinoplanes missouriensis
52400
-
x * 52400, His-tagged enzyme, sequence calculation, x * 53000, recombinant His-tagged enzyme, SDS-PAGE Streptomyces coelicolor
53000
-
x * 52400, His-tagged enzyme, sequence calculation, x * 53000, recombinant His-tagged enzyme, SDS-PAGE Streptomyces coelicolor
62000
-
x * 49800, His-tagged enzyme, sequence calculation, x * 62000, recombinant His-tagged enzyme, SDS-PAGE Actinoplanes missouriensis

Organism

Organism UniProt Comment Textmining
Actinoplanes missouriensis Q7WUM3 gene mak1
-
Streptomyces coelicolor O54204 gene pep2
-
Streptomyces coelicolor A3(2) O54204 gene pep2
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Streptomyces lividans strain 66 by nickel affinity chromatography Streptomyces coelicolor
recombinant His-tagged enzyme from Streptomyces lividans strain 66 by nickel affinity chromatography Actinoplanes missouriensis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
144.8
-
purified His-tagged recombinant enzyme, pH 7.0, 45°C Streptomyces coelicolor

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + maltose maltose cannot be replaced by spectinomycin, streptomycin, kasugamycin, kanamycin, hygromycin, or apramycin as a phosphoryl-group acceptor Actinoplanes missouriensis ADP + maltose 1-phosphate
-
?
ATP + maltose maltotriose, maltotetraose, L-arabinose, inositol, cellobiose, L-lactose, D-mannose, raffinose, or trehalose cannot replace maltose as a phosphorylgroup acceptor in the reaction catalyzed by Pep2. ATP cannot be replaced by other nucleotides as a phosphoryl-group donor Streptomyces coelicolor ADP + maltose 1-phosphate
-
?
ATP + maltose maltotriose, maltotetraose, L-arabinose, inositol, cellobiose, L-lactose, D-mannose, raffinose, or trehalose cannot replace maltose as a phosphorylgroup acceptor in the reaction catalyzed by Pep2. ATP cannot be replaced by other nucleotides as a phosphoryl-group donor Streptomyces coelicolor A3(2) ADP + maltose 1-phosphate
-
?

Subunits

Subunits Comment Organism
? x * 49800, His-tagged enzyme, sequence calculation, x * 62000, recombinant His-tagged enzyme, SDS-PAGE Actinoplanes missouriensis
? x * 52400, His-tagged enzyme, sequence calculation, x * 53000, recombinant His-tagged enzyme, SDS-PAGE Streptomyces coelicolor

Synonyms

Synonyms Comment Organism
Mak1
-
Actinoplanes missouriensis
Pep2
-
Streptomyces coelicolor

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
-
Streptomyces coelicolor

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
Streptomyces coelicolor

Cofactor

Cofactor Comment Organism Structure
ATP dependent on. ATP cannot be replaced by other nucleotides as a phosphoryl-group donor Streptomyces coelicolor

General Information

General Information Comment Organism
physiological function maltokinase is the enzyme responsible for the ATP-dependent formation of maltose 1-phosphate Actinoplanes missouriensis