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Information on EC 1.1.1.77 - lactaldehyde reductase
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EC Tree
1.1.1.77 lactaldehyde reductaseSpecify your search results
Word Map
- 1.1.1.77
- l-fucose
- l-1,2-propanediol
- l-rhamnose
-
nad-linked
-
dissimilation
- aldolase
- typhimurium
- l-lactate
-
metal-catalyzed
-
dinucleotide-linked
-
klebsiella
- subtilisin
- dihydroxyacetone
-
1-phosphate
- pneumoniae
- anaerobiosis
-
irretrievably
-
bacteriol
- zymomonas
-
six-carbon
-
rha
- mobilis
-
fuculose
-
noninducible
-
metal-binding
-
laczya
-
rhamnose-induced
-
permease
-
iron-containing
- synthesis
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
L-lactaldehyde:propanediol oxidoreductase, Propanediol oxidoreductase, propanediol:nicotinamide adenine dinucleotide (NAD) oxidoreductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L-lactaldehyde:propanediol oxidoreductase
-
-
-
-
Propanediol oxidoreductase
-
-
-
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propanediol:nicotinamide adenine dinucleotide (NAD) oxidoreductase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(R)[or (S)]-propane-1,2-diol + NAD+ = (R)[or (S)]-lactaldehyde + NADH + H+
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
(R)[or (S)]-propane-1,2-diol:NAD+ oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY
37250-15-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-propane-1,2-diol + NAD+
(R)-lactaldehyde + NADH
-
-
-
-
?
(R)-propane-1,2-diol + NAD+
(R)-lactaldehyde + NADH
-
acts only on L-isomer
-
-
?
(R)-propane-1,2-diol + NAD+
(R)-lactaldehyde + NADH
-
utilizes D- and L-lactaldehyde in the reverse direction equally well
-
-
r
(S)-propane-1,2-diol + NAD+
(S)-lactaldehyde + NADH
-
only L-propane-1,2-diol is oxidized
-
-
?
(S)-propane-1,2-diol + NAD+
(S)-lactaldehyde + NADH
-
anaerobically lactaldehyde is reduced to propane-1,2-diol in the L-fucose and L-rhamnose metabolism
-
-
?
(S)-propane-1,2-diol + NAD+
(S)-lactaldehyde + NADH
-
aerobically only mutant, strain 3 and 430, are capable of growth on 1,2-propanediol
-
-
?
(S)-propane-1,2-diol + NAD+
(S)-lactaldehyde + NADH
-
in the fermentative metabolism 1,2-propanediol is formed under phosphate limitation via the methylglyoxal by-pass
-
-
?
(S)-propane-1,2-diol + NAD+
(S)-lactaldehyde + NADH
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Embden-Meyerhof pathway for 6-deoxyhexose catabolism
-
-
?
L-1,2-propanediol + NAD+
L-lactaldehyde + NADH + H+
-
-
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-propane-1,2-diol + NAD+
(S)-lactaldehyde + NADH
-
anaerobically lactaldehyde is reduced to propane-1,2-diol in the L-fucose and L-rhamnose metabolism
-
-
?
(S)-propane-1,2-diol + NAD+
(S)-lactaldehyde + NADH
-
aerobically only mutant, strain 3 and 430, are capable of growth on 1,2-propanediol
-
-
?
(S)-propane-1,2-diol + NAD+
(S)-lactaldehyde + NADH
-
in the fermentative metabolism 1,2-propanediol is formed under phosphate limitation via the methylglyoxal by-pass
-
-
?
(S)-propane-1,2-diol + NAD+
(S)-lactaldehyde + NADH
-
Embden-Meyerhof pathway for 6-deoxyhexose catabolism
-
-
?
L-1,2-propanediol + NAD+
L-lactaldehyde + NADH + H+
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADP+
-
cell extracts also contain lactaldehyde reductase activity which utilizes either NADH or NADPH as electron donor
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ascorbate
-
0.025 mM FeCl3 and 0.035 mM ascorbate causes a 90% enzyme inactivation after 120 min = inactivation of metal-catalyzed oxidation; several amino-acids prevent the inactivation; under aerobic conditions 0.025 mM FeCl3 causes a 50% enzyme inactivation after 120 min
Fe2+
-
under anaerobic conditions 0.01 mM Fe2+ and 0.1 mM H2O2 had the effect of 85% enzyme inactivation after 2 min, with addition of 0.0001 mM catalase the inactivation is only 25% after 2 min and with addition of 0.01 mM superoxide dismutase instead of catalse the inactivation is again 82% after 2 min
Fe3+
-
0.025 mM FeCl3 and 0.035 mM ascorbate causes a 90% enzyme inactivation after 120 min = inactivation of metal-catalyzed oxidation; several amino-acids prevent the inactivation; under aerobic conditions 0.025 mM FeCl3 causes a 50% enzyme inactivation after 120 min
H2O2
-
under anaerobic conditions 0.01 mM Fe2+ and 0.1 mM H2O2 had the effect of 85% enzyme inactivation after 2 min, with addition of 0.0001 mM catalase the inactivation is only 25% after 2 min and with addition of 0.01 mM superoxide dismutase instead of catalse the inactivation is again 82% after 2 min
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
Lack of influence of the anaerobic [NiFe] hydrogenase and L-1,2 propanediol oxidoreductase on the outcome of Actinobacillus pleuropneumoniae serotype 7 infection.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 10
-
reduction of lactaldehyde, pH 4.5: 50% of reductase activity maximum, pH 10: 10% of reductase activity maximum
6 - 7.8
-
reduction of DL-lactaldehyde, pH 6: 50% of reductase activity maximum, pH 7.8: 45% of reductase activity maximum
8 - 11
-
dehydrogenation of 1,2-propanediol, pH 8: 10% of dehydrogenase activity maximum, pH 11: 65% of dehydrogenase activity maximum
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 43
25 - 43
-
optimal temperature for enzyme activity differs in various organisms
25 - 43
-
optimal temperature for enzyme activity differs in various organisms
25 - 43
-
optimal temperature for enzyme activity differs in various organisms
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Show AA Sequence and Transmembrane Helices (3105 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
76000
-
gel permeation chromatography on a calibrated column of Ultrogel AcA 34 under denaturating conditions
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
a rhaO knockout mutant produces reduced levels of L-1,2-propanediol during growth in rhamnose, the mutant cannot utilise rhamnose as the sole carbon source but grows normally on glucose
additional information
-
a rhaO knockout mutant produces reduced levels of L-1,2-propanediol during growth in rhamnose, the mutant cannot utilise rhamnose as the sole carbon source but grows normally on glucose
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crude extract, ammonium sulfate precipitation, heat treatment, ultrogel AcA 34 fractionation, DEAE-Sephadex column chromatography, second ultrogel AcA 34 fractionation
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crude extract, protamine sulfate, ammonium sulfate, DEAE-Sephadex-25, hydroxylapatite, blue dextran polyacrylamide
Microcyclus eburneus
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extraction, heat treatment, ammonium sulfate-fractionation, DEAE-cellulose and Alumina C
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene rhaO, encoded in the rhaKIPAO gene cluster, expression analysis, transcriptional regulation of the rhaKIPAOR gene cluster, overview
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
fermentation of L-rhamnose, L-fucose and D-fucose to a mixture of 1,2-propanediol, acetone, H2, CO2 and ethanol
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tran-Din, K.; Gottschalk, G.
Formation of D(-)-1,2-propanediol and D(-)-lactate from glucose by Clostridium sphenoides under phosphate limitation
Arch. Microbiol.
142
87-92
1985
Lacrimispora sphenoides
-
brenda
Ting, S.M.; Sellinger, O.Z.; Miller, O.N.
The metabolism of lactaldehyde VI. The reduction of D- and L-lactaldehyde in rat liver
Biochim. Biophys. Acta
89
217-225
1965
Rattus norvegicus
brenda
Kawagishi, T.; Nishio, N.; Matsuno, R.; Kamikubo, T.
Purification of NAD-dependent 1,2-propanediol dehydrogenating enzyme from Microcyclus eberneus
Agric. Biol. Chem.
44
949-950
1980
Microcyclus eburneus
-
brenda
Weimer, P.J.
Fermentation of 6-deoxyhexoses by Bacillus macerans
Appl. Environ. Microbiol.
47
263-267
1984
Paenibacillus macerans
brenda
Boronat, A.; Aguilar,J.
Rhamnose-induced propanediol oxidoreductase in Escherichia coli: purification, properties and comparison with the fucose-induced enzyme
J. Bacteriol.
140
320-326
1979
Escherichia coli
brenda
Hacking, A.J.; Lin, E.C.C.
Disruption of the fucose pathway as a consequence of genetic adaptation to propanediol as a carbon source in Escherichia coli
J. Bacteriol.
126
1166-1172
1976
Escherichia coli
brenda
Hacking, A.J.; Aguilar, J.; Lin, E.C.C.
Evolution of propanediol utilization in Escherichia coli: mutant with improved substrate-scavenging power
J. Bacteriol.
136
522-530
1978
Escherichia coli
brenda
Cocks, G.T.; Aguilar, J.; Lin, E.C.C.
Evolution of L-1,2-propanediol catabolism in Escherichia coli by recruitment of enzymes for L-fucose and L-lactate metabolism
J. Bacteriol.
118
83-88
1974
Escherichia coli
brenda
Boronat, A.; Aguilar, J.
Metabolism of L-fucose and L-rhamnose in Escherichia coli; differences in induction of propanediol oxidoreductase
J. Bacteriol.
147
181-185
1981
Escherichia coli
brenda
Cabiscol, E.; Badia, J.; Baldoma, L.; Hidalgo, E.; Aguilar, J.; Ros, J.
Inactivation of propanediol oxidoreductase of Escherichia coli by metal-catalyzed oxidation
Biochim. Biophys. Acta
1118
155-160
1992
Escherichia coli
brenda
Patel, E.H.; Paul, L.V.; Patrick, S.; Abratt, V.R.
Rhamnose catabolism in Bacteroides thetaiotaomicron is controlled by the positive transcriptional regulator RhaR
Res. Microbiol.
159
678-684
2008
Bacteroides thetaiotaomicron, Bacteroides thetaiotaomicron VPI-5482
brenda
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