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(R)-lactaldehyde + NAD+ + H2O
(R)-lactate + NADH + 2 H+
(S)-lactaldehyde + NAD(P)+ + H2O
(S)-lactate + NAD(P)H + 2 H+
-
-
-
?
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + H+
(S)-lactaldehyde + NADP+ + H2O
(S)-lactate + NADPH + 2 H+
acetaldehyde + NAD+
acetate + NADH + H+
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
acrylaldehyde + NAD+ + H2O
acrylate + NADH
19% activity compared to D-lactaldehyde
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
-
?
crotonaldehyde + NAD+ + H2O
crotonate + NADH
84% activity compared to D-lactaldehyde
-
-
?
D-lactaldehyde + NAD+ + H2O
D-lactate + NADH + H+
DL-glyceraldehyde + NAD+ + H2O
glycerate + NADH
97% activity compared to D-lactaldehyde
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
4% activity compared to D-lactaldehyde
-
-
?
glycoaldehyde + NAD+ + H2O
glycolate + NADH + H+
-
-
-
-
?
glycolaldehyde + NAD+ + H2O
glycolate + NADH
glycolaldehyde + NAD+ + H2O
glycolate + NADH + 2 H+
L-glyceraldehyde + NAD+ + H2O
L-glycerate + NADH
-
-
-
-
ir
L-lactaldehyde + NAD+ + H2O
L-lactate + NADH + H+
-
-
-
?
methylglyoxal + NAD+ + H2O
pyruvate + NADH
-
-
-
-
ir
p-methoxybenzaldehyde + NAD+ + H2O
p-methoxybenzoate + NADH + H+
-
-
-
-
?
p-nitrobenzaldehyde + NAD+ + H2O
p-nitrobenzoate + NADH + H+
-
-
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH
187% activity compared to D-lactaldehyde
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
-
-
-
-
?
propionaldehyde + NADP+ + H2O
propionate + NADPH + H+
-
ALD wild-type only uses NAD+. F180T mutation renders an enzyme with the ability to use NADP+
-
-
?
additional information
?
-
(R)-lactaldehyde + NAD+ + H2O
(R)-lactate + NADH + 2 H+
-
8.6% of the activity of (S)-lactaldehyde
-
-
?
(R)-lactaldehyde + NAD+ + H2O
(R)-lactate + NADH + 2 H+
-
8.6% of the activity of (S)-lactaldehyde
-
-
?
(R)-lactaldehyde + NAD+ + H2O
(R)-lactate + NADH + 2 H+
54% of the activity of L-lactaldehyde
-
-
?
(R)-lactaldehyde + NAD+ + H2O
(R)-lactate + NADH + 2 H+
75% of the activity of (S)-lactaldehyde
-
-
?
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
-
catabolism of L-threonine via amino acetone and methylglyoxal
-
-
?
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
-
essential for catabolism of 1,2-propanediol
-
-
?
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
-
aerobic metabolism of fucose
-
-
?
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
-
general role in aldehyde oxidation, involved in several metabolic pathways
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + H+
-
best substrate
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + H+
-
best substrate
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + H+
-
-
-
-
ir
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + H+
-
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + H+
-
-
-
-
ir
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + H+
-
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + H+
best substrate
-
-
?
(S)-lactaldehyde + NADP+ + H2O
(S)-lactate + NADPH + 2 H+
assay using NADP+
-
-
?
(S)-lactaldehyde + NADP+ + H2O
(S)-lactate + NADPH + 2 H+
assay using NADP+
-
-
?
acetaldehyde + NAD+
acetate + NADH + H+
-
-
-
?
acetaldehyde + NAD+
acetate + NADH + H+
-
-
-
?
acetaldehyde + NAD+
acetate + NADH + H+
-
-
-
?
acetaldehyde + NAD+
acetate + NADH + H+
-
-
-
?
acetaldehyde + NAD+
acetate + NADH + H+
-
-
-
?
acetaldehyde + NAD+
acetate + NADH + H+
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
25% activity compared to D-lactaldehyde
-
-
?
D-lactaldehyde + NAD+ + H2O
D-lactate + NADH + H+
-
56% the rate of L-lactaldehyde reduction
-
-
?
D-lactaldehyde + NAD+ + H2O
D-lactate + NADH + H+
-
-
-
?
D-lactaldehyde + NAD+ + H2O
D-lactate + NADH + H+
-
0.2% the activity of L-lactaldehyde reduction
-
-
?
glycolaldehyde + NAD+ + H2O
glycolate + NADH
-
-
-
-
?
glycolaldehyde + NAD+ + H2O
glycolate + NADH
-
-
-
-
ir
glycolaldehyde + NAD+ + H2O
glycolate + NADH
35% activity compared to D-lactaldehyde
-
-
?
glycolaldehyde + NAD+ + H2O
glycolate + NADH + 2 H+
-
-
-
-
?
glycolaldehyde + NAD+ + H2O
glycolate + NADH + 2 H+
-
-
-
-
?
glycolaldehyde + NAD+ + H2O
glycolate + NADH + 2 H+
-
-
-
?
additional information
?
-
-
oxidizes several aldehydes, e.g. L-glyceraldehyde, glycolaldehyde, methylglyoxal
-
-
?
additional information
?
-
-
not: acetaldehyde, formaldehyde, propionaldehyde, succinic semialdehyde
-
-
?
additional information
?
-
-
specifically oxidizes L-lactaldehyde to L-lactate in presence of NAD+
-
-
?
additional information
?
-
residue Asn286 of L-lactaldehyde dehydrogenase plays an important structure role to substrate identification. The wild-type enzyme is not active with D-glyceraldehyde, methylglyoxal, acetaldehyde, L-lactate, or benzaldehyde
-
-
?
additional information
?
-
-
residue Asn286 of L-lactaldehyde dehydrogenase plays an important structure role to substrate identification. The wild-type enzyme is not active with D-glyceraldehyde, methylglyoxal, acetaldehyde, L-lactate, or benzaldehyde
-
-
?
additional information
?
-
-
the enzyme shows NAD+-dependent l-lactaldehyde dehydrogenase activity in the methylglyoxyl metabolism, metabolizing methylglyoxal via methylglyoxal reductase and lactaldehyde dehydrogenase to L-lactate, overview
-
-
?
additional information
?
-
-
the enzyme shows NAD+-dependent l-lactaldehyde dehydrogenase activity in the methylglyoxyl metabolism, metabolizing methylglyoxal via methylglyoxal reductase and lactaldehyde dehydrogenase to L-lactate, overview
-
-
?
additional information
?
-
-
not: acetaldehyde, DL-glyceraldehyde, propionaldehyde, phenylpyruvate
-
-
?
additional information
?
-
-
specifically oxidizes L-lactaldehyde to L-lactate in presence of NAD+
-
-
?
additional information
?
-
-
the enzyme shows NAD+-dependent l-lactaldehyde dehydrogenase activity in the methylglyoxyl metabolism, metabolizing methylglyoxal via methylglyoxal reductase and lactaldehyde dehydrogenase to L-lactate, overview
-
-
?
additional information
?
-
-
the enzyme shows NAD+-dependent l-lactaldehyde dehydrogenase activity in the methylglyoxyl metabolism, metabolizing methylglyoxal via methylglyoxal reductase and lactaldehyde dehydrogenase to L-lactate, overview
-
-
?
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(S)-lactaldehyde + NAD(P)+ + H2O
(S)-lactate + NAD(P)H + 2 H+
-
-
-
?
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
additional information
?
-
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
-
catabolism of L-threonine via amino acetone and methylglyoxal
-
-
?
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
-
essential for catabolism of 1,2-propanediol
-
-
?
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
-
aerobic metabolism of fucose
-
-
?
(S)-lactaldehyde + NAD+
(S)-lactate + NADH
-
general role in aldehyde oxidation, involved in several metabolic pathways
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
-
-
-
?
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
-
-
-
-
?
additional information
?
-
-
the enzyme shows NAD+-dependent l-lactaldehyde dehydrogenase activity in the methylglyoxyl metabolism, metabolizing methylglyoxal via methylglyoxal reductase and lactaldehyde dehydrogenase to L-lactate, overview
-
-
?
additional information
?
-
-
the enzyme shows NAD+-dependent l-lactaldehyde dehydrogenase activity in the methylglyoxyl metabolism, metabolizing methylglyoxal via methylglyoxal reductase and lactaldehyde dehydrogenase to L-lactate, overview
-
-
?
additional information
?
-
-
the enzyme shows NAD+-dependent l-lactaldehyde dehydrogenase activity in the methylglyoxyl metabolism, metabolizing methylglyoxal via methylglyoxal reductase and lactaldehyde dehydrogenase to L-lactate, overview
-
-
?
additional information
?
-
-
the enzyme shows NAD+-dependent l-lactaldehyde dehydrogenase activity in the methylglyoxyl metabolism, metabolizing methylglyoxal via methylglyoxal reductase and lactaldehyde dehydrogenase to L-lactate, overview
-
-
?
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0.00048
-
whole cell lysate
0.355
purified recombinant enzyme, S-lactaldehyde, NADP+
0.6
100 mM TES pH 7.5, 2.5 mM NAD+
1.65
purified recombinant enzyme, (S)-lactaldehyde, NADP+
11.5
-
purified recombinant enzyme, glycolaldehyde, NAD+
17.2
-
purified recombinant enzyme, (S)-lactaldehyde, NAD+
2.1
purified recombinant enzyme, R-lactaldehyde, NAD+
2.28
-
purified recombinant enzyme, (R)-D-lactaldehyde, NAD+
3.64
purified recombinant enzyme, S-lactaldehyde, NAD+
4.28
purified recombinant enzyme, glycolaldehyde, NAD+
4.43
purified recombinant enzyme, (R)-lactaldehyde, NAD+
6.95
purified recombinant enzyme, (S)-lactaldehyde, NAD+
8.94
purified recombinant enzyme, glycolaldehyde, NAD+
additional information
-
-
0.00051
-
whole cell lysate
0.00051
-
whole cell lysate, procyclics
0.74
wild-type, pH 7.0, 37°C
0.74
purified recombinant enzyme, pH 7.0, 37°C, substrate (S)-lactaldehyde
1.18
mutant N286H, pH 7.0, 37°C
1.18
purified recombinant mutant N286H, pH 7.0, 37°C, substrate (S)-lactaldehyde
1.78
mutant N286H, pH 7.0, 37°C
1.78
purified recombinant mutant N286E, pH 7.0, 37°C, substrate (S)-lactaldehyde
2.18
mutant N286H, pH 7.0, 37°C
2.18
purified recombinant mutant N286T, pH 7.0, 37°C, substrate (S)-lactaldehyde
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F180T
-
renders an enzyme with the ability to use NADP+. NADP+ activity is higher than that attained with NAD+. Exhibits a 16fold increase in the Vm/Km ratio with NAD+ as the coenzyme. Absence of Mg2+ inhibitory effect on F180T activity
H449R
site-directed mutagenesis
L158Y
site-directed mutagenesis
N286A
site-directed mutagenesis
N286C
site-directed mutagenesis
N286D
site-directed mutagenesis
N286F
site-directed mutagenesis
N286G
site-directed mutagenesis
N286I
site-directed mutagenesis
N286K
site-directed mutagenesis
N286L
site-directed mutagenesis
N286M
site-directed mutagenesis
N286P
site-directed mutagenesis
N286Q
site-directed mutagenesis
N286R
site-directed mutagenesis
N286S
site-directed mutagenesis
N286V
site-directed mutagenesis
N286W
site-directed mutagenesis
N286Y
site-directed mutagenesis
N286E
engineering of L-lactaldehyde dehydrogenase. Contrary to wild-type, mutant is able to oxidate glyceraldehyde
N286E
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme and is able to oxidate glyceraldehyde and methylglyoxal
N286H
engineering of L-lactaldehyde dehydrogenase. Contrary to wild-type, mutant is able to oxidate glyceraldehyde
N286H
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme and is able to oxidate glyceraldehyde and methylglyoxal, as well as acetaldehyde
N286T
engineering of L-lactaldehyde dehydrogenase. Contrary to wild-type, mutant is able to oxidate glyceraldehyde. Compared to L-lactaldehyde, N286T has a one-third lower Km value to glyceraldehyde.
N286T
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme and is able to oxidate glyceraldehyde and methylglyoxal, as well as acetaldehyde
additional information
calculated Gibbs free energy of protein-substrate interaction of enzyme mutants with D-glyceraldehyde as substrate
additional information
-
calculated Gibbs free energy of protein-substrate interaction of enzyme mutants with D-glyceraldehyde as substrate
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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
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
Caballero, E.; Baldoma, L.; Ros, J.; Boronat, A.; Aguilar, J.
Identification of lactaldehyde dehydrogenase and glycolaldehyde dehydrogenase as functions of the same protein in Escherichia coli
J. Biol. Chem.
258
7788-7792
1983
Escherichia coli
brenda
Inoue, Y.; Watanabe, K.; Shimosaka, M.; Saikusa, T.; Fukuda, Y.; Murata, K.; Kimura, A.
Metabolism of 2-oxoaldehydes in yeasts. Purification and characterization of lactaldehyde dehydrogenase from Saccharomyces cerevisiae
Eur. J. Biochem.
153
243-247
1985
Saccharomyces cerevisiae
brenda
Baldoma, L.; Aguilar, J.
Involvement of lactaldehyde dehydrogenase in several metabolic pathways of Escherichia coli K12
J. Biol. Chem.
262
13991-13996
1987
Escherichia coli
brenda
Baldoma, L.; Aguilar, J.
Metabolism of L-fucose and L-rhamnose in Escherichia coli: aerobic-anaerobic regulation of L-lactaldehyde dissimilation
J. Bacteriol.
170
416-421
1988
Escherichia coli
brenda
Sridhara, S.; Wu, T.T.
Purification and properties of lactaldehyde dehydrogenase from Escherichia coli
J. Biol. Chem.
244
5233-5238
1969
Escherichia coli
brenda
Willetts, A.J.; Turner, J.M.
Threonine metabolism in a strain of Bacillus subtilis: enzymic oxidation of the intermediate DL-lactaldehyde
Biochim. Biophys. Acta
222
234-236
1970
Bacillus subtilis
brenda
Rodriguez-Zavala, J.S.; Allali-Hassani, A.; Weiner, H.
Characterization of E. coli tetrameric aldehyde dehydrogenases with atypical properties compared to other aldehyde dehydrogenases
Protein Sci.
15
1387-1396
2006
Escherichia coli
brenda
Grochowski, L.L.; Xu, H.; White, R.H.
Identification of lactaldehyde dehydrogenase in Methanocaldococcus jannaschii and its involvement in production of lactate for F420 biosynthesis
J. Bacteriol.
188
2836-2844
2006
Methanocaldococcus jannaschii (Q58806), Methanocaldococcus jannaschii
brenda
Di Costanzo, L.; Gomez, G.A.; Christianson, D.W.
Crystal structure of lactaldehyde dehydrogenase from Escherichia coli and inferences regarding substrate and cofactor specificity
J. Mol. Biol.
366
481-493
2006
Escherichia coli (P25553), Escherichia coli
brenda
Greig, N.; Wyllie, S.; Patterson, S.; Fairlamb, A.H.
A comparative study of methylglyoxal metabolism in trypanosomatids
FEBS J.
276
376-386
2009
Leishmania major, Trypanosoma brucei, Trypanosoma cruzi
brenda
Rodriguez-Zavala, J.S.
Enhancement of coenzyme binding by a single point mutation at the coenzyme binding domain of E. coli lactaldehyde dehydrogenase
Protein Sci.
17
563-570
2008
Escherichia coli
brenda
Watanabe, S.; Piyanart, S.; Makino, K.
Metabolic fate of L-lactaldehyde derived from an alternative L-rhamnose pathway
FEBS J.
275
5139-5149
2008
Azotobacter vinelandii, Scheffersomyces stipitis, Scheffersomyces stipitis (A3LNE3), Scheffersomyces stipitis (A3M013), Azotobacter vinelandii NBRC 102612
brenda
Wu, X.; Xu, L.; Yan, M.
A new NAD(+)-dependent glyceraldehyde dehydrogenase obtained by rational design of l-lactaldehyde dehydrogenase from Escherichia coli
Biosci. Biotechnol. Biochem.
80
2306-2310
2016
Escherichia coli (P25553), Escherichia coli
brenda
Wu, X.; Xu, L.; Yan, M.
A new NAD+-dependent glyceraldehyde dehydrogenase obtained by rational design of l-lactaldehyde dehydrogenase from Escherichia coli
Biosci. Biotechnol. Biochem.
80
2306-2310
2016
Escherichia coli (P25553), Escherichia coli
brenda
Wolf, J.; Stark, H.; Fafenrot, K.; Albersmeier, A.; Pham, T.K.; Mueller, K.B.; Meyer, B.H.; Hoffmann, L.; Shen, L.; Albaum, S.P.; Kouril, T.; Schmidt-Hohagen, K.; Neumann-Schaal, M.; Braesen, C.; Kalinowski, J.; Wright, P.C.; Albers, S.V.; Schomburg, D.; Siebers, B.
A systems biology approach reveals major metabolic changes in the thermoacidophilic archaeon Sulfolobus solfataricus in response to the carbon source L-fucose versus D-glucose
Mol. Microbiol.
102
882-908
2016
Saccharolobus solfataricus (Q97UA1), Saccharolobus solfataricus P2 (Q97UA1)
brenda
MacCabe, A.; Sanmartin, G.; Orejas, M.
Identification of the genes encoding the catalytic steps corresponding to LRA4 (l-2-keto-3-deoxyrhamnonate aldolase) and L-lactaldehyde dehydrogenase in Aspergillus nidulans evidence for involvement of the loci AN9425/lraD and AN0544/aldA in the L-rhamnose catabolic pathway
Environ. Microbiol.
23
2420-2432
2021
Aspergillus nidulans (Q5BFY6), Aspergillus nidulans, Aspergillus nidulans ATCC 38163 (Q5BFY6), Aspergillus nidulans CBS 112.46 (Q5BFY6), Aspergillus nidulans FGSC A4 (Q5BFY6), Aspergillus nidulans M139 (Q5BFY6), Aspergillus nidulans NRRL 194 (Q5BFY6)
brenda
MacCabe,A.; Sanmartin, G.; Orejas, M.
Identification of the genes encoding the catalytic steps corresponding to LRA4 (l-2-keto-3-deoxyrhamnonate aldolase) and L-lactaldehyde dehydrogenase in Aspergillus nidulans evidence for involvement of the loci AN9425/lraD and AN0544/aldA in the l-rhamnose catabolic pathway
Environ. Microbiol.
2021
2420-2432
2021
Aspergillus nidulans (A0A1U8QKS3), Aspergillus nidulans, Aspergillus nidulans ATCC 38163 (A0A1U8QKS3)
brenda