Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.1.1.2 - alcohol dehydrogenase (NADP+) and Organism(s) Thermoanaerobacter brockii and UniProt Accession P14941

for references in articles please use BRENDA:EC1.1.1.2
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
A zinc protein. Some members of this group oxidize only primary alcohols; others act also on secondary alcohols. May be identical with EC 1.1.1.19 (L-glucuronate reductase), EC 1.1.1.33 [mevaldate reductase (NADPH)] and EC 1.1.1.55 [lactaldehyde reductase (NADPH)]. Re-specific with respect to NADPH.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Thermoanaerobacter brockii
UNIPROT: P14941
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Thermoanaerobacter brockii
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
nadph-cytochrome c reductase, aldo-keto reductase, liver alcohol dehydrogenase, adh-1, adh-2, short-chain alcohol dehydrogenase, lbadh, nadph-dependent aldehyde reductase, cbadh, tsadh319, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-DG-reducing enzyme
-
-
-
-
Alcohol dehydrogenase [NADP+]
-
-
-
-
aldehyde reductase
-
-
-
-
aldehyde reductase (NADPH2)
-
-
-
-
Aldo-keto reductase family 1 member A1
-
-
-
-
ALR
-
-
-
-
ALR 1
-
-
-
-
high-Km aldehyde reductase
-
-
-
-
low-Km aldehyde reductase
-
-
-
-
NADP-alcohol dehydrogenase
-
-
-
-
NADP-aldehyde reductase
-
-
-
-
NADP-dependent aldehyde reductase
-
-
-
-
NADPH-aldehyde reductase
-
-
-
-
NADPH-dependent aldehyde reductase
-
-
-
-
nonspecific succinic semialdehyde reductase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a primary alcohol + NADP+ = an aldehyde + NADPH + H+
show the reaction diagram
thermodynamics, standard electromotive force for reduction of NADP+ is -0.140 V
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
alcohol:NADP+ oxidoreductase
A zinc protein. Some members of this group oxidize only primary alcohols; others act also on secondary alcohols. May be identical with EC 1.1.1.19 (L-glucuronate reductase), EC 1.1.1.33 [mevaldate reductase (NADPH)] and EC 1.1.1.55 [lactaldehyde reductase (NADPH)]. Re-specific with respect to NADPH.
CAS REGISTRY NUMBER
COMMENTARY hide
9028-12-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-butanol + NADP+
?
show the reaction diagram
-
-
-
?
2-butanol + NADP+
butan-2-one + NADPH
show the reaction diagram
-
-
-
-
r
2-propanol + NADP+
acetone + NADPH
show the reaction diagram
-
-
-
-
r
acetone + NADPH + H+
propan-2-ol + NADP+
show the reaction diagram
-
about 13% of the activity with butan-2-ol
-
-
?
butan-2-ol + NADP+
butanone + NADPH + H+
show the reaction diagram
-
good substrate
-
-
r
butanone + NADPH + H+
butan-2-ol + NADP+
show the reaction diagram
-
-
-
-
r
cyclohexanol + NADP+
cyclohexanone + NADPH + H+
show the reaction diagram
-
about 15% of the activity with butan-2-ol
-
-
?
cyclopentanol + NADP+
cyclopentanal + NADPH
show the reaction diagram
-
-
-
-
r
ethanol + NADP+
acetaldehyde + NADPH + H+
show the reaction diagram
-
-
-
-
r
pent-1-en-3-ol + NADP+
pent-1-en-3-one + NADPH + H+
show the reaction diagram
-
good substrate
-
-
?
propan-2-ol + NADP+
acetone + NADPH + H+
show the reaction diagram
-
good substrate
-
-
?
additional information
?
-
-
activity of the reversible enzyme is highest for secondary alcohols and decreases in order of acetaldehyde, linear ketones, cyclic ketones and primary alcohols. It is active on five- to seven-membered ring ketones but not with cyclo-octanone as substrate
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-propanol + NADP+
acetone + NADPH
show the reaction diagram
-
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
-
dependent on
NADPH
additional information
-
no activity with NAD(H)
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-chloromercuribenzoate
-
1 mM, complete inactivation
acetone
-
at high concentrations of e.g. 3.4 M
additional information
-
not inhibitory: EDTA (5 mM), MgCl2 (10 mM), CaCl2 (1O mM), CuCl2 (1 mM) and ZnCl2 (1 mM)
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7 - 9.2
2-butanol
0.7
acetone
-
pH 7.8, 40°C
0.31
butan-2-ol
-
pH 7.8, 40°C
0.12
Butanone
-
pH 7.8, 40°C
8.45 - 19.33
Cyclopentanol
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
-
more than 50% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at room temperature
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ADH_THEBR
352
0
37647
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
150000
-
gel filtration
40000
-
4 * 40000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of P275D–TbADH1 are grown using the hanging-drop vapor-diffusion method at 20°C. Crystal structure of the thermostabilized mutant P275D-EhADH1 suggests that a proline residue at position 275 thermostabilizes the enzymes by reducing flexibility and by reinforcing hydrophobic interactions at the dimer–dimer interface of the tetrameric ADH
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
P275D
mutation reduces the thermostability of the enzyme
additional information
-
evaluation of a dehydrogenase-acetone NADP-regeneration system for the enzymatic preparative-scale production of 12-ketochenodeoxycholic acid, overview
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
76
1 h, 50% loss of activity of wild-type enzyme
87
1 h, 50% loss of activity of mutant enzyme D275P
65
-
70 min, no loss of activity
98
-
half-life 1-2 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
1 unit of ADH dissolved in 0.5 ml of 0.1 M potassium phosphate buffer, pH 8.0, containing 4% w/v cholic acid 100 mM, 100 mM NADP+, 1 mM dithiothreitol, and 10% or 25% v/v acetone, 23 days, quite stable
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type and mutant enzyme
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli, wild-type and mutant enzyme
gene coding for TBADH cloned and overexpressed in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
the enzyme is utilized in a dehydrogenase-acetone NADP-regeneration system for the enzymatic preparative-scale production of 12-ketochenodeoxycholic acid, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bryant, F.O.; Wiegel, J.; Ljungdahl, L.G.
Purification and properties of primary and secondary alcohol dehydrogenases from Thermoanaerobacter ethanolicus
Appl. Environ. Microbiol.
2
460-465
1988
Acinetobacter sp., Geobacillus stearothermophilus, Saccharomyces cerevisiae, Clostridium beijerinckii, Thermoanaerobacter brockii, Thermoanaerobacter thermohydrosulfuricus, Escherichia coli, Thermoanaerobacter ethanolicus, Zymomonas mobilis
-
Manually annotated by BRENDA team
Burdette, D.; Zeikus, J.G.
Purification of acetaldehyde dehydrogenase and alcohol dehydrogenases from Thermoanaerobacter ethanolicus 39E and characterization of the secondary-alcohol dehydrogenase (2 degrees Adh) as a bifunctional alcohol dehydrogenase-acetyl-CoA reductive thioesterase
Biochem. J.
302
163-170
1994
Leuconostoc mesenteroides, Saccharomyces cerevisiae, Clostridium acetobutylicum, Clostridium beijerinckii, Thermoanaerobacter brockii, Clostridium kluyveri, Acetivibrio thermocellus, Thermoanaerobacter thermohydrosulfuricus, Escherichia coli, Propionibacterium freudenreichii, Thermoanaerobacter ethanolicus, Vibrio harveyi, Zymomonas mobilis, Clostridium acetobutylicum NRRL B643, Clostridium beijerinckii NRRL B592, Thermoanaerobacter ethanolicus JW 200
Manually annotated by BRENDA team
Ma, K.; Robb, F.T.; Adams, M.W.
Purification and characterization of NADP-specific alcohol dehydrogenase and glutamate dehydrogenase from the hyperthermophilic archaeon Thermococcus litoralis
Appl. Environ. Microbiol.
60
562-568
1994
Acetobacter aceti, Saccharomyces cerevisiae, Thermoanaerobacter brockii, Drosophila melanogaster, Methanobacterium palustre, Methanofollis liminatans, Methanoculleus thermophilus, Thermococcus litoralis, Zymomonas mobilis
Manually annotated by BRENDA team
Bogin, O.; Peretz, M.; Burstein, Y.
Thermoanaerobacter brockii alcohol dehydrogenase: characterization of the active site metal and its ligand amino acids
Protein Sci.
6
450-458
1997
Saccharomyces cerevisiae, Thermoanaerobacter brockii, Equus sp., Homo sapiens
Manually annotated by BRENDA team
Peralba, J.M.; Cederlund, E.; Crosas, B.; Moreno, A.; Julia, P.; Martinez, S.E.; Persson, B.; Farr s, J.; Pares, X.; Jornvall, H.
Structural and enzymatic properties of a gastric NADP(H)-dependent and retinal-active alcohol dehydrogenase
J. Biol. Chem.
274
26021-26026
1999
Clostridium beijerinckii, Thermoanaerobacter brockii, Entamoeba histolytica, Pelophylax perezi, Thermoanaerobacter ethanolicus
Manually annotated by BRENDA team
Li, C.; Heatwole, J.; Soelaiman, S.; Shoham, M.
Crystal structure of a thermophilic alcohol dehydrogenase substrate complex suggests determinants of substrate specificity and thermostability
Proteins
37
619-627
1999
Thermoanaerobacter brockii
Manually annotated by BRENDA team
King, M.T.
Thermodynamics of the reduction of NADP with 2-propanol catalyzed by an NADP-dependent alcohol dehydrogenase
Arch. Biochem. Biophys.
410
280-286
2003
Thermoanaerobacter brockii
Manually annotated by BRENDA team
Fossati, E.; Polentini, F.; Carrea, G.; Riva, S.
Exploitation of the alcohol dehydrogenase-acetone NADP-regeneration system for the enzymatic preparative-scale production of 12-ketochenodeoxycholic acid
Biotechnol. Bioeng.
93
1216-1220
2006
Thermoanaerobacter brockii, Levilactobacillus brevis
Manually annotated by BRENDA team
Goihberg, E.; Dym, O.; Tel-Or, S.; Shimon, L.; Frolow, F.; Peretz, M.; Burstein, Y.
Thermal stabilization of the protozoan Entamoeba histolytica alcohol dehydrogenase by a single proline substitution
Proteins
72
711-719
2008
Thermoanaerobacter brockii (P14941), Thermoanaerobacter brockii, Entamoeba histolytica (P35630), Entamoeba histolytica
Manually annotated by BRENDA team
Lamed, R.J.; Zeikus, J.G.
Novel NADP-linked alcohol-aldehyde/ketone oxidoreductase in thermophilic ethanologenic bacteria
Biochem. J.
195
183-190
1981
Thermoanaerobacter brockii
Manually annotated by BRENDA team