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Information on EC 2.7.1.175 - maltokinase and Organism(s) Actinoplanes missouriensis and UniProt Accession Q7WUM3

for references in articles please use BRENDA:EC2.7.1.175
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IUBMB Comments
Requires Mg2+ for activity.
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Select one or more organisms in this record:
This record set is specific for:
Actinoplanes missouriensis
UNIPROT: Q7WUM3
Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The taxonomic range for the selected organisms is: Actinoplanes missouriensis
Synonyms
ATP:maltose 1-phosphotransferase, Mak, Mak1, maltose-1-phosphate synthetase, Pep2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mak1
294995
gene name
SYSTEMATIC NAME
IUBMB Comments
ATP:alpha-maltose 1-phosphotransferase
Requires Mg2+ for activity.
CAS REGISTRY NUMBER
COMMENTARY hide
179987-43-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + maltose
ADP + maltose 1-phosphate
show the reaction diagram
maltose cannot be replaced by spectinomycin, streptomycin, kasugamycin, kanamycin, hygromycin, or apramycin as a phosphoryl-group acceptor
-
-
?
ATP + maltose
ADP + maltose 1-phosphate
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
-
dependent on, ATP is not replaceable as phosphoryl-group donor
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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.54
ATP
-
pH 8.5, 22°C
2.6
maltose
-
pH 8.5, 22°C
additional information
additional information
-
Michaelis-Menten kinetics
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.75
-
in Tris/HCl buffer
8.5
-
in TEA/HCl buffer
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the activity of maltokinase increases 2.5fold with a maximum at 55°C, but decreases rapidly at temperatures above 60°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.3
-
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene mak1
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
maltokinase is the enzyme responsible for the ATP-dependent formation of maltose 1-phosphate
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
MAK_ACTMI
437
0
47731
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49800
x * 49800, His-tagged enzyme, sequence calculation, x * 62000, recombinant His-tagged enzyme, SDS-PAGE
62000
x * 49800, His-tagged enzyme, sequence calculation, x * 62000, recombinant His-tagged enzyme, SDS-PAGE
57000
-
1 * 57000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 49800, His-tagged enzyme, sequence calculation, x * 62000, recombinant His-tagged enzyme, SDS-PAGE
monomer
-
1 * 57000, SDS-PAGE
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Streptomyces lividans strain 66 by nickel affinity chromatography
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
-
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Niehues, B.; Jossek, R.; Kramer, U.; Koch, A.; Jarling, M.; Schroeder, W.; Pape, H.
Isolation and characterization of maltokinase (ATP:maltose 1-phosphotransferase) from Actinoplanes missouriensis
Arch. Microbiol.
180
233-239
2003
Actinoplanes missouriensis
Manually annotated by BRENDA team
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
J. Basic Microbiol.
44
360-373
2004
Actinoplanes missouriensis, Actinoplanes missouriensis (Q7WUM3), Streptomyces coelicolor (O54204), Streptomyces coelicolor, Streptomyces coelicolor A3(2) (O54204)
Manually annotated by BRENDA team
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