Information on EC 1.1.1.244 - methanol dehydrogenase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY hide
1.1.1.244
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RECOMMENDED NAME
GeneOntology No.
methanol dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
methanol + NAD+ = formaldehyde + NADH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
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Methane metabolism
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methanol oxidation to carbon dioxide
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methanol oxidation to formaldehyde II
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
methanol:NAD+ oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY hide
74506-37-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strains NRIC0498T, LMG1667 and NRIC0554
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Manually annotated by BRENDA team
strain C1
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Manually annotated by BRENDA team
ATCC53907, three isozymes, two of the genes are encoded on the chromosome and one on a plasmid
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Manually annotated by BRENDA team
NCIMB13113, three isozymes, two of the genes are encoded on the chromosome and one on a plasmid
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Manually annotated by BRENDA team
strains B18LD and OH75-2a
UniProt
Manually annotated by BRENDA team
strain MP2, isolated from seawater, gene mxaF
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Manually annotated by BRENDA team
strain MP2, isolated from seawater, gene mxaF
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Manually annotated by BRENDA team
strain MP1, isolated from seawater, gene mxaF
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Manually annotated by BRENDA team
strain MP1, isolated from seawater, gene mxaF
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Manually annotated by BRENDA team
sp. nov., isolated from seawater, gene mxaF
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Manually annotated by BRENDA team
strain BG8
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Manually annotated by BRENDA team
strain BG8
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Manually annotated by BRENDA team
Methylomicrobium sp.
strain HG-1
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Manually annotated by BRENDA team
strain HG-1
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Manually annotated by BRENDA team
Methylophaga spp.
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Manually annotated by BRENDA team
no activity in Acetobacter lovaniensis
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Manually annotated by BRENDA team
no activity in Acetobacter malorum
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Manually annotated by BRENDA team
no activity in Acetobacter malorum DSM14337T
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Manually annotated by BRENDA team
no activity in Acetobacter pomorum
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Manually annotated by BRENDA team
no activity in Acetobacter pomorum DSM11825T
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,3-propandiol + NAD+
? + NADH + H+
show the reaction diagram
butanol + NAD+
butanal + NADH + H+
show the reaction diagram
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?
ethanol + NAD+
acetaldehyde + NADH + H+
show the reaction diagram
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r
ethanol + NAD+
ethanal + NADH
show the reaction diagram
formaldehyde + NADH + H+
methanol + NAD+
show the reaction diagram
isopropanol + NAD+
isopropanal + NADH + H+
show the reaction diagram
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low activity
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?
methanol + NAD+
formaldehyde + NADH + H+
show the reaction diagram
n-butanol + NAD+
n-butanal + NADH
show the reaction diagram
n-propanol + NAD+
n-propanal + NADH
show the reaction diagram
octanol + NAD+
octanal + NADH
show the reaction diagram
propanol + NAD+
propanal + NADH + H+
show the reaction diagram
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?
additional information
?
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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
ethanol + NAD+
ethanal + NADH
show the reaction diagram
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methanol + NAD+
formaldehyde + NADH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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reduction of aldehyde
EDTA
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reduction of aldehyde
iodoacetate
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weak inhibition of aldehyde reduction
N-ethylmaleimide
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weak inhibition of aldehyde reduction
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Activator protein
activator protein ACT
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all three isozymes are activated by ACT, which is encoded by gene act, overview
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NudF protein
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can be catalytically stimulated by the Bacillus subtilis NudF protein in vitro
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additional information
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strongly stimulated by the ACT protein
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1 - 7.1
formaldehyde
0.02 - 2.5
NAD+
additional information
additional information
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.2
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enzyme activity in crude extracts of methanol grown cells, fully activated enzyme, enzyme activity is 10fold lower in the absence of activator protein
19.6
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formaldehyde reductase activity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
Methylomicrobium sp.
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
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activity optimum at about 45C for all isozymes
60
Methylomicrobium sp.
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4
Methylomicrobium sp.
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
71000
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SDS-PAGE and mass spectrometry
120000
Methylomicrobium sp.
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gel filtration
363000
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ultracentrifugation sedimentation equilibrium, dissociation occurs during the centrifugation time of 80 h
430000
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calculated from electron microscopic analysis and MW of subunit
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decamer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
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20 min, the isozymes are all stable up to; 20 min, the isozymes are stable up to, except for isozyme Mdh1, which shows about 35-40% loss of activity
50
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t1/2: above 2 min
70
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t1/2: 2 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dilution inactivates methanol dehydrogenase activity, not reductase activity, sucrose, 20% w/v, stabilizes formaldehyde reductase not methanol dehydrogenase activity, metal ions, such as Fe2+ and Zn2+, do not stabilize methanol dehydrogenase activity, glycerol does not stabilize methanol dehydrogenase activity, dithiothreitol stabilizes reductase, not methanol dehydrogenase activity, storage leads to dissociation
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80 to 4C, in the presence of DTT at least 4 days stable
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4-20C, complete dissociation after 48 h
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4-20C, enzyme dissociates upon storage
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gel filtration
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native and recombinant proteins
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purification of activator protein
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Q-Sepharose, Phenyl-Superose, dehydrogenase activity is almost completely lost after purification, 34% reductase activity are recovered
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wild type and mutant enzymes
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli DH5alpha
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expressed in Escherichia coli, full activity only when grown in Mg2+ containing medium
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gene mxaF, DNA and amino acid sequence determination and analysis, genotypic and phylogenetic analysis and species verfication, overview
three isozymes, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain ER2566
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D100N
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strongly reduced NAD+-binding, no activity
D88N
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only minor effects on activity
G13A
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only minor effects on activity
G15A
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only minor effects on activity
G95A
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impaired cofactor binding, low acitivity
K103R
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strongly reduced NAD+-binding, no activity
S97G
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impaired cofactor binding, much higher acitivity than the wild type enzyme, no activation with ACT protein
S97T
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impaired cofactor binding, much higher acitivity than the wild type enzyme, no activation with ACT protein
Show AA Sequence (178 entries)
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