BRENDA - Enzyme Database
show all sequences of 2.7.1.175

Isolation and characterization of maltokinase (ATP:maltose 1-phosphotransferase) from Actinoplanes missouriensis

Niehues, B.; Jossek, R.; Kramer, U.; Koch, A.; Jarling, M.; Schroeder, W.; Pape, H.; Arch. Microbiol. 180, 233-239 (2003)

Data extracted from this reference:

KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten kinetics
Actinoplanes missouriensis
0.54
-
ATP
pH 8.5, 22°C
Actinoplanes missouriensis
2.6
-
maltose
pH 8.5, 22°C
Actinoplanes missouriensis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Actinoplanes missouriensis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
57000
-
1 * 57000, SDS-PAGE
Actinoplanes missouriensis
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Actinoplanes missouriensis
-
-
-
Purification (Commentary)
Commentary
Organism
native enzyme by heat treatment at 50°C for 30 min, anion exchange chromatography, ammonium sulfate fractionation, hydrophobic interaction chromatography, ultra- and gel filtration, and another step of anion exchange chromatography
Actinoplanes missouriensis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + maltose
-
717163
Actinoplanes missouriensis
ADP + maltose 1-phosphate
-
-
-
?
Subunits
Subunits
Commentary
Organism
monomer
1 * 57000, SDS-PAGE
Actinoplanes missouriensis
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
55
-
-
Actinoplanes missouriensis
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
additional information
-
the activity of maltokinase increases 2.5fold with a maximum at 55°C, but decreases rapidly at temperatures above 60°C
Actinoplanes missouriensis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.75
-
in Tris/HCl buffer
Actinoplanes missouriensis
8.5
-
in TEA/HCl buffer
Actinoplanes missouriensis
Cofactor
Cofactor
Commentary
Organism
Structure
ATP
dependent on, ATP is not replaceable as phosphoryl-group donor
Actinoplanes missouriensis
additional information
CTP and TTP show no activity, while GTP with 2.1% activity compared to ATP and UTP with 2.7% show only poor activity as phosphoryl-group donors
Actinoplanes missouriensis
pI Value
Organism
Commentary
pI Value Maximum
pI Value
Actinoplanes missouriensis
isoelectric focusing
-
4.3
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
ATP
dependent on, ATP is not replaceable as phosphoryl-group donor
Actinoplanes missouriensis
additional information
CTP and TTP show no activity, while GTP with 2.1% activity compared to ATP and UTP with 2.7% show only poor activity as phosphoryl-group donors
Actinoplanes missouriensis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten kinetics
Actinoplanes missouriensis
0.54
-
ATP
pH 8.5, 22°C
Actinoplanes missouriensis
2.6
-
maltose
pH 8.5, 22°C
Actinoplanes missouriensis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Actinoplanes missouriensis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
57000
-
1 * 57000, SDS-PAGE
Actinoplanes missouriensis
Purification (Commentary) (protein specific)
Commentary
Organism
native enzyme by heat treatment at 50°C for 30 min, anion exchange chromatography, ammonium sulfate fractionation, hydrophobic interaction chromatography, ultra- and gel filtration, and another step of anion exchange chromatography
Actinoplanes missouriensis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + maltose
-
717163
Actinoplanes missouriensis
ADP + maltose 1-phosphate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1 * 57000, SDS-PAGE
Actinoplanes missouriensis
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
55
-
-
Actinoplanes missouriensis
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
additional information
-
the activity of maltokinase increases 2.5fold with a maximum at 55°C, but decreases rapidly at temperatures above 60°C
Actinoplanes missouriensis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.75
-
in Tris/HCl buffer
Actinoplanes missouriensis
8.5
-
in TEA/HCl buffer
Actinoplanes missouriensis
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Actinoplanes missouriensis
isoelectric focusing
-
4.3
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
-
-
-
-
-
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
-
-
-
-
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
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-