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Information on EC 1.2.1.7 - benzaldehyde dehydrogenase (NADP+)
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EC Tree
1.2.1.7 benzaldehyde dehydrogenase (NADP+)Specify your search results
Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
ppbadh, 4-hydroxy benzaldehyde dehydrogenase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
mdlD
NAD(P)-dependent benzaldehyde dehydrogenase
NADP-linked benzaldehyde dehydrogenase
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-
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PpBADH
additional information
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
benzaldehyde + NADP+ + H2O = benzoate + NADPH + H+
inducible by mandelic acid
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benzaldehyde + NADP+ + H2O = benzoate + NADPH + H+
inducible by xenobiotics, like DDT and TCDD
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benzaldehyde + NADP+ + H2O = benzoate + NADPH + H+
inducible by xenobiotics, like DDT and TCDD
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benzaldehyde + NADP+ + H2O = benzoate + NADPH + H+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
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reduction
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oxidation
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
benzaldehyde:NADP+ oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY
9028-89-1
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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
2,4-dihydroxybenzaldehyde + NAD+ + H2O
2,4-dihydroxybenzoate + NADH + H+
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-
-
-
?
3,4-dihydroxybenzaldehyde + NAD+ + H2O
3,4-dihydroxybenzoate + NADH + H+
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-
-
-
?
3-hydroxy-4-methoxybenzaldehyde + NAD+ + H2O
3-hydroxy-4-methoxybenzoate + NADH + H+
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-
-
-
?
3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + H+
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-
-
-
?
3-methoxybenzaldehyde + NAD+ + H2O
3-methoxybenzoate + NADH + H+
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-
-
-
?
4-hydroxy-3-methoxybenzaldehyde + NAD+ + H2O
4-hydroxy-3-methoxybenzoate + NADH + H+
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-
-
-
?
4-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoate + NADH + H+
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-
-
-
?
isovanillin + NADP+ + H2O
3-hydroxy-4-methoxybenzoate + NADPH
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-
-
-
?
4-chlorobenzaldehyde + H2O + NADP+
4-chlorobenzoate + NADPH + 2 H+
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-
-
?
4-chlorobenzaldehyde + H2O + NADP+
4-chlorobenzoate + NADPH + 2 H+
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-
-
?
4-hydroxybenzaldehyde + NADP+ + H2O
4-hydroxybenzoate + NADPH + H+
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-
-
?
4-hydroxybenzaldehyde + NADP+ + H2O
4-hydroxybenzoate + NADPH + H+
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-
-
?
4-methoxybenzaldehyde + H2O + NADP+
4-methoxybenzoate + NADPH + 2 H+
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-
-
?
4-methoxybenzaldehyde + H2O + NADP+
4-methoxybenzoate + NADPH + 2 H+
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-
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?
4-nitrobenzaldehyde + H2O + NADP+
4-nitrobenzoate + NADPH + 2 H+
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-
-
?
4-nitrobenzaldehyde + H2O + NADP+
4-nitrobenzoate + NADPH + 2 H+
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-
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?
benzaldehyde + H2O + NADP+
benzoate + NADPH + 2 H+
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?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
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Pseudomonas enzyme on plasmid also active with NAD+, see also EC 1.2.1.28
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ir
benzaldehyde + NADP+ + H2O
benzoate + NADPH
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metabolic pathway of mandelic acid
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?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
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metabolic pathway of phenylglycine
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?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
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metabolic pathway of phenylglycine
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?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
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Pseudomonas enzyme on plasmid also active with NAD+, see also EC 1.2.1.28
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ir
additional information
?
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specificity data for PpBADH shows that long chain aliphatics containing 5-8 carbons have about twice the relative rate of reactivity than benzaldehyde. As the chain length decreases, the activity declines quickly, with less than 0.1% activity being observed with acetaldehyde. Structure-function analysis
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additional information
?
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specificity data for PpBADH shows that long chain aliphatics containing 5-8 carbons have about twice the relative rate of reactivity than benzaldehyde. As the chain length decreases, the activity declines quickly, with less than 0.1% activity being observed with acetaldehyde. Structure-function analysis
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additional information
?
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specificity data for PpBADH shows that long chain aliphatics containing 5-8 carbons have about twice the relative rate of reactivity than benzaldehyde. As the chain length decreases, the activity declines quickly, with less than 0.1% activity being observed with acetaldehyde. Structure-function analysis
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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
4-hydroxybenzaldehyde + NADP+ + H2O
4-hydroxybenzoate + NADPH + H+
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-
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?
4-hydroxybenzaldehyde + NADP+ + H2O
4-hydroxybenzoate + NADPH + H+
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-
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?
benzaldehyde + H2O + NADP+
benzoate + NADPH + 2 H+
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-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
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Pseudomonas enzyme on plasmid also active with NAD+, see also EC 1.2.1.28
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ir
benzaldehyde + NADP+ + H2O
benzoate + NADPH
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metabolic pathway of mandelic acid
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?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
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metabolic pathway of phenylglycine
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?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
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metabolic pathway of phenylglycine
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?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
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Pseudomonas enzyme on plasmid also active with NAD+, see also EC 1.2.1.28
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ir
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
PpBADH is able to utilize both NAD+ and NADP+, selective mechanism, overview
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additional information
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PpBADH is able to utilize both NAD+ and NADP+, selective mechanism, overview
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
Rb+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
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IMAC eluted 4-hydroxy benzaldehyde dehydrogenase, total activity 35 Units, protein concentration 0.27 mg/ml
3.2
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clarified lysate, total activity 37 U, protein concentration 5.77 mg/ml
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
9.3
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.9 - 10.7
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the activities measured at pH 6.85 and 10.7 are approximately 30% of the activity measured at pH 9.3
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
early eosinophilic focus, basophilic adenoma and hepatocellular carcinom
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
additional information
evolution
benzaldehyde dehydrogenase from Pseudomonas putida (PpBADH) belongs to the Class 3 aldehyde dehydrogenase (ALDH) family. The Class 3 ALDHs are unusual in that they are generally dimeric (rather than tetrameric), relatively non-specific and utilize both NAD+ and NADP+. The pattern of cofactor binding for the rat Class 3 ALDH differs from that of PpBADH and other ALDHs
evolution
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benzaldehyde dehydrogenase from Pseudomonas putida (PpBADH) belongs to the Class 3 aldehyde dehydrogenase (ALDH) family. The Class 3 ALDHs are unusual in that they are generally dimeric (rather than tetrameric), relatively non-specific and utilize both NAD+ and NADP+. The pattern of cofactor binding for the rat Class 3 ALDH differs from that of PpBADH and other ALDHs
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metabolism
benzaldehyde dehydrogenase (PpBADH) is the terminal enzyme in the mandelamide/mandelate pathway of Pseudomonas putida strain ATCC 12633, it catalyzes the conversion of benzaldehyde to benzoic acid with the concomitant reduction of NAD+ (EC 1.2.1.28) or NADP+ (EC 1.2.1.7) to NADH or NADPH, respectively. Benzoic acid subsequently enters the beta-oxoadipate pathway and the citric acid cycle
metabolism
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benzaldehyde dehydrogenase (PpBADH) is the terminal enzyme in the mandelamide/mandelate pathway of Pseudomonas putida strain ATCC 12633, it catalyzes the conversion of benzaldehyde to benzoic acid with the concomitant reduction of NAD+ (EC 1.2.1.28) or NADP+ (EC 1.2.1.7) to NADH or NADPH, respectively. Benzoic acid subsequently enters the beta-oxoadipate pathway and the citric acid cycle
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additional information
two conserved glutamates, at positions 215 and 337, act as the general base necessary to hydrolyze the thioacyl intermediate, structure-activity relationship, mechanism, overview. Glu215 is the likely candidate for PpBADH, a result more typical of the Class 1 and 2 ALDH families. Hydride transfer is not rate limiting, lending further credence to the suggestion that PpBADH is more similar to the Class 1 and 2 ALDHs than it is to other Class 3 ALDHs. Structure comparisons
additional information
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two conserved glutamates, at positions 215 and 337, act as the general base necessary to hydrolyze the thioacyl intermediate, structure-activity relationship, mechanism, overview. Glu215 is the likely candidate for PpBADH, a result more typical of the Class 1 and 2 ALDH families. Hydride transfer is not rate limiting, lending further credence to the suggestion that PpBADH is more similar to the Class 1 and 2 ALDHs than it is to other Class 3 ALDHs. Structure comparisons
additional information
-
two conserved glutamates, at positions 215 and 337, act as the general base necessary to hydrolyze the thioacyl intermediate, structure-activity relationship, mechanism, overview. Glu215 is the likely candidate for PpBADH, a result more typical of the Class 1 and 2 ALDH families. Hydride transfer is not rate limiting, lending further credence to the suggestion that PpBADH is more similar to the Class 1 and 2 ALDHs than it is to other Class 3 ALDHs. Structure comparisons
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). AL3B1_BOVIN
468
0
51800
Swiss-Prot
other Location (Reliability: 4)
AL3B1_HUMAN
468
0
51840
Swiss-Prot
Mitochondrion (Reliability: 4)
AL3B1_MOUSE
468
0
52292
Swiss-Prot
other Location (Reliability: 2)
AL3B1_RAT
468
0
52147
Swiss-Prot
other Location (Reliability: 3)
A0A1J5S9M2_9ZZZZ
459
0
51315
TrEMBL
other Location (Reliability: 2)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme in complex with NADP+ and NADP+/benzoate, sitting drop vapour diffusion method, mixing of 10 mg/ml protein in 100 mM HEPES, 100 mM KCl, 2 mM DTT, 2 mM NADP+, pH 7.5, and 1 mM benzoate (for the complex cyrstals), with crystallization solution containing 2.0 M ammonium sulfate and 5% v/v isopropanol, 5-7 days, X-ray diffraction structure determination and analysis at 2.28 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E215D
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
E337D
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
E337L
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
E337Q
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
E215D
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site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
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E337D
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site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
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E337Q
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site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
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additional information
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random mutagenesis of plasmid encoded benzaldehyde dehydrogenase gene xylC, expression in Escherichia coli
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE