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Information on EC 1.1.1.2 - alcohol dehydrogenase (NADP+) and Organism(s) Entamoeba histolytica and UniProt Accession P35630

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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.
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Entamoeba histolytica
UNIPROT: P35630
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The taxonomic range for the selected organisms is: Entamoeba histolytica
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
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ADH
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Alcohol dehydrogenase [NADP+]
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aldehyde reductase
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aldehyde reductase (NADPH2)
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Aldo-keto reductase family 1 member A1
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ALR
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ALR 1
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high-Km aldehyde reductase
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low-Km aldehyde reductase
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NADP-alcohol dehydrogenase
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NADP-aldehyde reductase
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NADP-dependent aldehyde reductase
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NADPH-aldehyde reductase
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NADPH-dependent aldehyde reductase
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nonspecific succinic semialdehyde reductase
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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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
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-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ADH1_ENTHI
360
0
38568
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
130000
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gel filtration
30000
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4 * 30000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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crystallization data
tetramer
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4 * 30000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of D275P–EhADH1 are grown using the hanging-drop vapor-diffusion method at 20°C. Crystal structure of the thermostabilized mutant D275P-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
D275P
mutation significantly enhances the thermal stability of EhADH1
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type and mutant enzyme
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli, wild-type and mutant enzyme
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Lo, H.S.; Chang, C.J.
Purification and properties of NADP-linked, alcohol dehydrogenase from Entamoeba histolytica
J. Parasitol.
68
372-377
1982
Entamoeba histolytica, Homo sapiens
Manually annotated by BRENDA team
Shimon, L.J.; Peretz, M.; Goihberg, E.; Burstein, Y.; Frolow, F.
Thermophilic alcohol dehydrogenase from the mesophile Entamoeba histolytica: crystallization and preliminary X-ray characterization
Acta Crystallogr. Sect. D
58
546-548
2002
Entamoeba histolytica
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