BRENDA - Enzyme Database
show all sequences of 2.7.1.175

Isolation of mak1 from Actinoplanes missouriensis and evidence that Pep2 from Streptomyces coelicolor is a maltokinase

Jarling, M.; Cauvet, T.; Grundmeier, M.; Kuhnert, K.; Pape, H.; J. Basic Microbiol. 44, 360-373 (2004)

Data extracted from this reference:

Cloned(Commentary)
Commentary
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
Commentary
Organism
Structure
Mg2+
required
Streptomyces coelicolor
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
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
Primary Accession No. (UniProt)
Commentary
Textmining
Actinoplanes missouriensis
Q7WUM3
gene mak1
-
Streptomyces coelicolor
O54204
gene pep2
-
Streptomyces coelicolor A3(2)
O54204
gene pep2
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged enzyme from Streptomyces lividans strain 66 by nickel affinity chromatography
Actinoplanes missouriensis
recombinant His-tagged enzyme from Streptomyces lividans strain 66 by nickel affinity chromatography
Streptomyces coelicolor
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
144.8
-
purified His-tagged recombinant enzyme, pH 7.0, 45°C
Streptomyces coelicolor
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + maltose
maltose cannot be replaced by spectinomycin, streptomycin, kasugamycin, kanamycin, hygromycin, or apramycin as a phosphoryl-group acceptor
717739
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
717739
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
717739
Streptomyces coelicolor A3(2)
ADP + maltose 1-phosphate
-
-
-
?
Subunits
Subunits
Commentary
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
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
45
-
-
Streptomyces coelicolor
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
-
Streptomyces coelicolor
Cofactor
Cofactor
Commentary
Organism
Structure
ATP
dependent on. ATP cannot be replaced by other nucleotides as a phosphoryl-group donor
Streptomyces coelicolor
Cloned(Commentary) (protein specific)
Commentary
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
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
ATP
dependent on. ATP cannot be replaced by other nucleotides as a phosphoryl-group donor
Streptomyces coelicolor
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Streptomyces coelicolor
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
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
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged enzyme from Streptomyces lividans strain 66 by nickel affinity chromatography
Actinoplanes missouriensis
recombinant His-tagged enzyme from Streptomyces lividans strain 66 by nickel affinity chromatography
Streptomyces coelicolor
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
144.8
-
purified His-tagged recombinant enzyme, pH 7.0, 45°C
Streptomyces coelicolor
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + maltose
maltose cannot be replaced by spectinomycin, streptomycin, kasugamycin, kanamycin, hygromycin, or apramycin as a phosphoryl-group acceptor
717739
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
717739
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
717739
Streptomyces coelicolor A3(2)
ADP + maltose 1-phosphate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
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
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
45
-
-
Streptomyces coelicolor
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
-
Streptomyces coelicolor
General Information
General Information
Commentary
Organism
physiological function
maltokinase is the enzyme responsible for the ATP-dependent formation of maltose 1-phosphate
Actinoplanes missouriensis
General Information (protein specific)
General Information
Commentary
Organism
physiological function
maltokinase is the enzyme responsible for the ATP-dependent formation of maltose 1-phosphate
Actinoplanes missouriensis
Other publictions for EC 2.7.1.175
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
739666
Fraga
Structure of mycobacterial mal ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618, Mycolicibacterium vanbaalenii, Mycolicibacterium vanbaalenii DSM 7251
Sci. Rep.
5
8026
2015
-
-
2
1
15
-
-
-
-
2
-
4
-
6
-
-
2
1
-
-
-
-
4
1
3
-
-
-
2
-
-
2
-
-
-
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-
2
2
1
15
-
-
-
-
-
-
2
-
4
-
-
-
2
-
-
-
-
4
1
3
-
-
-
2
-
-
-
-
5
5
-
-
-
737320
Roy
Synthesis of alpha-glucan in m ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618
ACS Chem. Biol.
8
2245-2255
2013
1
-
1
-
3
-
-
1
-
1
3
2
-
7
-
-
1
-
-
-
-
-
2
2
-
-
-
-
1
-
-
1
-
-
-
1
-
1
1
-
3
-
-
-
-
1
-
1
3
2
-
-
-
1
-
-
-
-
2
2
-
-
-
-
1
-
-
-
-
3
3
-
-
-
717432
Mendes
Biochemical characterization o ...
Mycobacterium tuberculosis variant bovis
BMC Biochem.
11
21
2010
-
1
1
-
-
1
1
3
-
5
1
1
-
5
-
-
1
-
-
-
-
1
4
1
1
1
-
-
1
1
-
3
-
-
-
-
1
1
3
-
-
1
-
1
-
3
-
5
1
1
-
-
-
1
-
-
-
1
4
1
1
1
-
-
1
1
-
-
-
2
2
-
-
-
717816
Elbein
Last step in the conversion of ...
Mycolicibacterium smegmatis, Mycolicibacterium smegmatis ATCC 14468
J. Biol. Chem.
285
9803-9812
2010
-
1
-
-
-
-
-
-
-
1
-
-
-
4
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
1
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1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
1
1
-
-
-
717739
Jarling
Isolation of mak1 from Actinop ...
Actinoplanes missouriensis, Streptomyces coelicolor, Streptomyces coelicolor A3(2)
J. Basic Microbiol.
44
360-373
2004
-
-
2
-
-
-
-
-
-
1
4
-
-
9
-
-
2
-
-
-
1
-
3
2
1
-
-
-
1
-
-
1
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
1
4
-
-
-
-
2
-
-
1
-
3
2
1
-
-
-
1
-
-
-
-
1
1
-
-
-
717163
Niehues
Isolation and characterization ...
Actinoplanes missouriensis
Arch. Microbiol.
180
233-239
2003
-
-
-
-
-
-
-
3
-
1
1
-
-
2
-
-
1
-
-
-
-
-
1
1
1
1
-
-
2
-
-
2
-
1
-
-
-
-
2
-
-
-
-
-
-
3
-
1
1
-
-
-
-
1
-
-
-
-
1
1
1
1
-
-
2
-
-
1
-
-
-
-
-
-
717600
Drepper
Maltokinase (ATP:maltose 1-pho ...
Actinoplanes sp.
FEBS Lett.
388
177-179
1996
-
-
-
-
-
-
-
-
-
1
-
1
-
2
-
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-
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2
-
1
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-
1
-
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1
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1
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1
-
1
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2
-
1
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-
1
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-
-
-
-
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