Information on EC 3.6.3.19 - maltose-transporting ATPase

Word Map on EC 3.6.3.19
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY hide
3.6.3.19
-
RECOMMENDED NAME
GeneOntology No.
maltose-transporting ATPase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + maltose/out = ADP + phosphate + maltose/in
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
transmembrane transport
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (maltose-importing)
ABC-type (ATP-binding cassette-type) ATPase, characterized by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. Comprises bacterial enzymes that import maltose and maltose oligosaccharides.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
genes malEFG
-
-
Manually annotated by BRENDA team
genes malEFG
-
-
Manually annotated by BRENDA team
serovar typhimurium
-
-
Manually annotated by BRENDA team
contains the maltose ABC transporter system encoded by malEFG-a
-
-
Manually annotated by BRENDA team
contains the maltose ABC transporter system encoded by malEFG-a
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
the enzyme is a member of the ATP-binding cassette superfamily
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
maltose binding protein
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Aes
-
antagonizing maltotriose binding by MalT
-
alpha-cyclodextrin
-
-
antibody 4H12
-
recognizes the peptide 111-NQRVNQVAEVLQL-123
-
antibody 5B5
-
recognizes the peptide 53-ETITSGDLTRM-67
-
beta-cyclodextrin
-
-
EIIAGlc
-
when glucose as preferred carbon source is transported, EIIAGlc becomes predominantly unphosphorylated and allosterically inhibits several permeases, including MalFGK2, which possesses a specific binding site in region III of EIIAGlc, in a process termed inducer exclusion involving the N-terminal part of the inhibitor, binding surface, overview
-
enzyme IIAglc
-
-
-
gamma-cyclodextrin
-
-
MalK
-
0.008 mM, in the absence of maltotriose 80% inhibition, no inhibition in the presence of 0.1 mM maltotriose
-
MalY
-
antagonizing maltotriose binding by MalT
-
NaN3
-
FGK2 complex
p-Chloromercuriphenyl sulfonic acid
-
FGK2 complex
vanadate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
MalF
-
MalF stimulates the substrate transport activity through its second periplasmic loop, overview
-
maltose-binding protein
-
substrate-binding protein MalE
-
binds with high-affinity to MalFGK2 and facilitate the acquisition of maltose
-
verapamil
-
stimulates detergent-soluble maltose transporter, increases ATPase activity and lowers affinity for ATP
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1 - 0.33
ATP
0.0005 - 0.0075
maltose
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
avermectin production by wild-type and malEFG-a utant strains, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2
-
maltose transport assay
7.4
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at, enzyme reconstituted in proteoliposomes
23
-
assay at
25
-
assay at
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
the majority of the maltose binding protein is distributed throughout the cell wall, while only smaller quantities are located in the cytoplasmic membrane
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42000
-
x * 42000, SDS-PAGE
42977
x * 42977, calculated from nucleotide sequence
170000
-
tetrameric FGK2 complex, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
multimer
-
the maltose transporter consists of a periplasmic maltose binding protein and a multisubunit membrane transporter, MalFGK2
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis of full transporter MalFGK2 and of the MalF subunit
-
crystal structure analysis, e.g. of the crystal structure of the complex in the presence of ATP and MalE, containing MalK mutant E159Q, is resolved at 2.8 A, revealing that MalFG are in a periplasmically open state
-
enzyme IIA in complex with the maltose transporter, vapor diffusion method, using 100 mM sodium cacodylate pH 5.6, 13% (w/v) PEG monomethylether 2000 and 100 mM NDSB-256
-
MalK crystal structure analysis in the semi-open, nucleotide-free, the open nucleotide-free, the ATP-bound, and the ADP-bound states
-
pre-translocation, outward- and inward-facing crystal structure analysis of enzyme complex with or without bound maltose binding protein and bound maltose and ATP, overview
-
purified native MalFGK2 and and selenium methionine-labeled MalFGK2, in 20 mM Tris, pH 8.0, 50 mM NaCl, and 0.03% n-undecyl-beta-D-maltopyranoside, addtion of 5 mM 2-mercaptoethanol and 5 mM DTT for the SeMet-enzyme. Mixing of 1 mg/ml protein and reservoir solution, containing 11.5% PEG 4000, 0.1M N-(2-acetamido)iminodiacetic acid, pH 6.5, 0.1 M NaCl, and 0.1 M Li2SO4, in a 2:1 ratio, at 20C in sitting drops, crystals appear after 24 h and grow to full size within 1 week, X-ray diffraction structure determination and anaylsis at 2.8 A resolution
-
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
MgATP2-, binding protects against trypsin inactivation in wild-type enzyme in in G137 mutants
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cobalt resin column chromatography and Talon resin column chromatography
-
cobalt-affinity column chromatography and Superdex 200 gel filtration
-
maltose binding protein MalE
-
Ni-NTA-agarose microcolumn chromatography
-
Ni2+-chelating affinity gel chromatography and gel filtration
-
Ni2+-chelating column chromatography and Superdex 200HR gel filtration
-
purification of recombinant subunits
-
recombinant His-tagged enzyme from Escherichia coli strain JM109
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain JM109 by nickel affinity chromatography and ultrafiltration
recombinant wild-type and mutant MalFGK2 from Escherichia coli strain AD110 by cobalt affinity chromatography and gel filtration
-
wild-type strain and mutant strain that does not require maltose-binding protein for transport
-
with the aid of a glutathione S-transferase molecular tag
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Corynebacterium glutamicum strain IMcg2701
expressed in Escherichia coli BL21 Star (DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli strain RB791/pMBPHis6x
-
expression in Escherichia coli
expression in Escherichia coli strain AD110
-
expression in strain HN741
-
genes malEFG-a, encoding the maltose ABC transporter system, transcriptional analysis of malE-a by RT-PCR, and malEFG-a gene replacement cloning
-
maltose-binding protein MalE expressed in Escherichia coli
-
overexpression of His-tagged wild-type and mutant enzymes in Escherichia coli strain JM109
overexpression of MalF in Escherichia coli strain BL21(DE3)
-
recombinant His-tagged enzyme expression in Escherichia coli strain JM109
the type I maltose ABC importer is encoded within the maltose regulon
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of malE-a is induced by maltose
expression of malE-a is strongly repressed by glucose
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C40S/S83C
-
site-directed mutagenesis, the mutant shows altered subunit interactions in the maltose ABC transporter MALFGK2-E
D380G
-
substitution of aspartate for glycine in the maltose-binding site of MalF likely generates a futile cycle by preventing maltose from binding to MalFGK2 during the catalytic cycle
E159
-
the E159Q substitution in MalK prevents ATP from being hydrolysed. This results in an ATP-bound structure, which is thought to represent the transition state for ATP hydrolysis. The crystal shows an open (unliganded) MalE bound to the periplasmic side of the complex, a maltose molecule bound solely to a transmembrane region of MalF, and a closed conformation of the ATP-bound MalK(E59Q)2 subunits
E159Q
-
the transporter containing the MalK-E159Q mutation is defective in ATP hydrolysis
E313C
-
leads to a disulfide bond, no effect to ATPase activity
S205C/S252C
-
site-directed mutagenesis, the mutant shows altered subunit interactions in the maltose ABC transporter MALFGK2-E
T31C/S205C
-
site-directed mutagensis, formation of a crosslink betwwen the mutant subunits
T31C/T177C
-
site-directed mutagenesis, the distance between MalF mutant and MalE T31C mutant changes from 10 A to 5 A upon binding of ATP or maltose, with a less pronounced result, and is reset to 10 A after hydrolysis of one ATP
T80C/S205C
-
site-directed mutagenesis, the mutation of subunit MalF mutant S205C does not affect the interaction with MalE mutant T80C
W230C
-
site-directed mutagenesis, mutation in the maltose binding protein, the mutant shows altered kinetics of substrate binding compared to the wild-type maltose binding protein
W340C
-
site-directed mutagenesis, mutation in the maltose binding protein, the mutant shows altered kinetics of substrate binding compared to the wild-type maltose binding protein
W62C
-
site-directed mutagenesis, mutation in the maltose binding protein, the mutant shows altered kinetics of substrate binding compared to the wild-type maltose binding protein, but retains good function in maltose transport and MBP-stimulated ATPase activities
Y155C
-
site-directed mutagenesis, mutation in the maltose binding protein, the mutant shows altered kinetics of substrate binding compared to the wild-type maltose binding protein
Y341C
-
site-directed mutagenesis, mutation in the maltose binding protein, the mutant shows altered kinetics of substrate binding compared to the wild-type maltose binding protein, but retaines good function in maltose transport and MBP-stimulated ATPase activities
T31C/S205C
-
site-directed mutagensis, formation of a crosslink betwwen the mutant subunits
T31C/T177C
-
site-directed mutagenesis, the distance between MalF mutant and MalE T31C mutant changes from 10 A to 5 A upon binding of ATP or maltose, with a less pronounced result, and is reset to 10 A after hydrolysis of one ATP
T80C/S205C
-
site-directed mutagenesis, the mutation of subunit MalF mutant S205C does not affect the interaction with MalE mutant T80C
G137A
-
mutation in MalK, fails to restore a functional transport complex in vivo, mutation increases the repressing activity of MalK on other maltose-regulated genes, loss of ability to hydrolyze ATP, but still displays nucleotide-binding activity
G137T
-
mutation in MalK, fails to restore a functional transport complex in vivo, mutation increases the repressing activity of MalK on other maltose-regulated genes, loss of ability to hydrolyze ATP, but still displays nucleotide-binding activity
G137V
-
mutation in MalK, fails to restore a functional transport complex in vivo, mutation increases the repressing activity of MalK on other maltose-regulated genes, loss of ability to hydrolyze ATP, but still displays nucleotide-binding activity
Q140L
-
mutation in MalK, fails to restore a functional transport complex in vivo, mutation increases the repressing activity of MalK on other maltose-regulated genes, fails to hydrolyze ATP and exhibits a strong intrinsic resistance to trypsin in the absence of MgATP, suggesting a drastically altered conformation
Q140N
-
mutation in MalK, fails to restore a functional transport complex in vivo, mutation increases the repressing activity of MalK on other maltose-regulated genes, ATPase activity and MgATP-induced changes in tryptic cleavage pattern similar to those of wild-type. Mutant transport complexes containing MalKQ140N variant, when studied in proteoliposomes, are severely impaired in MalE-maltose-stimulated ATPase activity
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant purified MalFGK2 are reconstituted into proteoliposomes at a lipid-to-protein ratio of 100:1 in g/ml
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
synthesis
Show AA Sequence (1890 entries)
Please use the Sequence Search for a specific query.