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EC Tree
IUBMB Comments The enzyme forms a bifunctional complex with EC 4.1.3.43, 4-hydroxy-2-oxohexanoate aldolase, with a tight channel connecting the two subunits [1,2,3]. Also acts, more slowly, on glycolaldehyde and butanal. In Pseudomonas species the enzyme forms a bifunctional complex with EC 4.1.3.39, 4-hydroxy-2-oxovalerate aldolase. The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 1.2.1.10, acetaldehyde dehydrogenase (acetylating). NADP+ can replace NAD+ with a much slower rate .
The enzyme appears in viruses and cellular organisms
Synonyms
BphJ, CoA-acylating aldehyde dehydrogenase, coenzyme A-acylating aldehyde dehydrogenase, More,
PduP , TTHB247,
more
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CoA-acylating aldehyde dehydrogenase
coenzyme A-acylating aldehyde dehydrogenase
additional information
-
cf. EC 1.2.1.57
BphJ
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-
CoA-acylating aldehyde dehydrogenase
-
-
CoA-acylating aldehyde dehydrogenase
-
CoA-acylating aldehyde dehydrogenase
-
-
CoA-acylating aldehyde dehydrogenase
-
-
coenzyme A-acylating aldehyde dehydrogenase
-
-
coenzyme A-acylating aldehyde dehydrogenase
-
coenzyme A-acylating aldehyde dehydrogenase
-
-
coenzyme A-acylating aldehyde dehydrogenase
-
-
PduP
-
-
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propanal + CoA + NAD+ = propanoyl-CoA + NADH + H+
-
-
-
-
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propanal:NAD+ oxidoreductase (CoA-propanoylating)
The enzyme forms a bifunctional complex with EC 4.1.3.43, 4-hydroxy-2-oxohexanoate aldolase, with a tight channel connecting the two subunits [1,2,3]. Also acts, more slowly, on glycolaldehyde and butanal. In Pseudomonas species the enzyme forms a bifunctional complex with EC 4.1.3.39, 4-hydroxy-2-oxovalerate aldolase. The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 1.2.1.10, acetaldehyde dehydrogenase (acetylating). NADP+ can replace NAD+ with a much slower rate [3].
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acetaldehyde + CoA + NAD+
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NADP+
acetyl-CoA + NADPH + H+
BphJ is able to utilize NAD+ and NADP+ with comparable kcat values, but the apparent Km-value for NAD+ is 16fold lower than for NADP+
-
-
?
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
butanoyl-CoA + NADH + H+
butanal + CoA + NAD+
butyraldehyde + CoA + NAD+
butyryl-CoA + NADH + H+
-
-
-
?
isobutyraldehyde + CoA + NAD+
isobutyryl-CoA + NADH + H+
-
-
-
?
pentaldehyde + CoA + NAD+
pentanoyl-CoA + NADH + H+
-
-
-
?
propanal + CoA + NAD+
propanoyl-CoA + NADH + H+
-
-
-
?
propanoyl-CoA + NADH + H+
propanal + CoA + NAD+
propionaldehyde + CoA + NAD+
propanoyl-CoA + NADH + H+
additional information
?
-
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH + H+
-
-
-
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH + H+
-
-
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH + H+
-
-
-
?
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
-
-
-
-
r
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
low activity
-
-
r
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
preferred substrate
-
-
r
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
low activity
-
-
r
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
preferred substrate
-
-
r
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
-
-
-
-
r
butanoyl-CoA + NADH + H+
butanal + CoA + NAD+
-
high activity
-
-
r
butanoyl-CoA + NADH + H+
butanal + CoA + NAD+
-
-
-
r
butanoyl-CoA + NADH + H+
butanal + CoA + NAD+
-
-
-
r
butanoyl-CoA + NADH + H+
butanal + CoA + NAD+
-
-
-
-
r
propanoyl-CoA + NADH + H+
propanal + CoA + NAD+
-
best substrate
-
-
r
propanoyl-CoA + NADH + H+
propanal + CoA + NAD+
best substrate
-
-
r
propanoyl-CoA + NADH + H+
propanal + CoA + NAD+
best substrate
-
-
r
propanoyl-CoA + NADH + H+
propanal + CoA + NAD+
-
best substrate
-
-
r
propionaldehyde + CoA + NAD+
propanoyl-CoA + NADH + H+
-
-
-
-
?
propionaldehyde + CoA + NAD+
propanoyl-CoA + NADH + H+
-
-
-
?
propionaldehyde + CoA + NAD+
propanoyl-CoA + NADH + H+
-
-
-
?
additional information
?
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-
substrate chain length specificity of the enzyme is C2-C12, overview
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-
?
additional information
?
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substrate chain length specificity of the enzyme is C2-C12, overview
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-
?
additional information
?
-
substrate chain length specificity of the enzyme is C2-C12, overview
-
-
?
additional information
?
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no activity with succinic semialdehyde and picolinaldehyde
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-
?
additional information
?
-
-
substrate chain length specificity of the enzyme is C2-C12, overview
-
-
?
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acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
butanoyl-CoA + NADH + H+
butanal + CoA + NAD+
propanal + CoA + NAD+
propanoyl-CoA + NADH + H+
-
-
-
?
propanoyl-CoA + NADH + H+
propanal + CoA + NAD+
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
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-
-
-
r
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
low activity
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-
r
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
low activity
-
-
r
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
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-
-
-
r
butanoyl-CoA + NADH + H+
butanal + CoA + NAD+
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high activity
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-
r
butanoyl-CoA + NADH + H+
butanal + CoA + NAD+
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-
-
r
butanoyl-CoA + NADH + H+
butanal + CoA + NAD+
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-
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r
butanoyl-CoA + NADH + H+
butanal + CoA + NAD+
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-
-
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r
propanoyl-CoA + NADH + H+
propanal + CoA + NAD+
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best substrate
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-
r
propanoyl-CoA + NADH + H+
propanal + CoA + NAD+
best substrate
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-
r
propanoyl-CoA + NADH + H+
propanal + CoA + NAD+
best substrate
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-
r
propanoyl-CoA + NADH + H+
propanal + CoA + NAD+
-
best substrate
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-
r
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NAD+
BphJ is able to utilize NAD+ and NADP+ with comparable kcat values, but the apparent Km-value for NAD+ is 16fold lower than for NADP+
NADP+
BphJ is able to utilize NAD+ and NADP+ with comparable kcat values, but the apparent Km-value for NAD+ is 16fold lower than for NADP+
NADH
-
-
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0.0926 - 0.342
acetyl-CoA
0.056 - 0.087
butanoyl-CoA
31.7
Butyraldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
7.7
Isobutyraldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
0.0348
NAD+
app. Km-value with acetaldehyde as substrate, pH 8.0 and 25°C
0.561
NADP+
app. Km-value with acetaldehyde as substrate, pH 8.0 and 25°C
additional information
additional information
Michaelis-Menten kientics
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5.5
acetaldehyde
app. Km-value, single TTHB247, pH 8.0, 25°C
7.4
acetaldehyde
-
I195L mutant, steady state, pH 8.0, 25°C
9.4
acetaldehyde
app. Km-value, TTHB247-BphI complex, pH 8.0, 25°C
15.4
acetaldehyde
app. Km-value, TTHB246-TTHB247 complex, pH 8.0, 25°C
15.7
acetaldehyde
app. Km-value, BphJ-TTHB246 complex, pH 8.0, 25°C
23.6
acetaldehyde
app. Km-value, BphJ-BphI complex, pH 8.0, 25°C
23.6
acetaldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
24
acetaldehyde
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wild-type protein, steady state, pH 8.0, 25°C
35
acetaldehyde
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I195F mutant, steady state, pH 8.0, 25°C
0.0926
acetyl-CoA
recombinant enzyme, pH 7.15, 30°C
0.181
acetyl-CoA
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recombinant enzyme, pH 7.15, 30°C
0.342
acetyl-CoA
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recombinant enzyme, pH 7.15, 30°C
0.056
butanoyl-CoA
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recombinant enzyme, pH 7.15, 30°C
0.0717
butanoyl-CoA
recombinant enzyme, pH 7.15, 30°C
0.087
butanoyl-CoA
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recombinant enzyme, pH 7.15, 30°C
2 - 3
propionaldehyde
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wild-type protein, steady state, pH 8.0, 25°C
6.4
propionaldehyde
app. Km-value, single TTHB247, pH 8.0, 25°C
7.7
propionaldehyde
-
I195L mutant, steady state, pH 8.0, 25°C
9.6
propionaldehyde
app. Km-value, TTHB247-BphI complex, pH 8.0, 25°C
16.1
propionaldehyde
app. Km-value, BphJ-TTHB246 complex, pH 8.0, 25°C
16.1
propionaldehyde
app. Km-value, TTHB246-TTHB247 complex, pH 8.0, 25°C
23.1
propionaldehyde
app. Km-value, BphJ-BphI complex, pH 8.0, 25°C
23.1
propionaldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
48
propionaldehyde
-
I195F mutant, steady state, pH 8.0, 25°C
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7.02 - 25.38
butanoyl-CoA
9.5
Butyraldehyde
pH 8.0 and 25°C, NAD+
11.2
Isobutyraldehyde
pH 8.0 and 25°C, NAD+
14.1
NAD+
with acetaldehyde as substrate, pH 8.0 and 25°C
12.9
NADP+
with acetaldehyde as substrate, pH 8.0 and 25°C
2.2
acetaldehyde
BphJ-TTHB246 complex, pH 8.0, 25°C
2.8
acetaldehyde
TTHB247-BphI complex, pH 8.0, 25°C
3.5
acetaldehyde
TTHB246-TTHB247 complex, pH 8.0, 25°C
7.4
acetaldehyde
single TTHB247, pH 8.0, 25°C
16
acetaldehyde
-
I195F mutant, steady state, pH 8.0, 25°C
17.2
acetaldehyde
BphJ-BphI complex, pH 8.0, 25°C
17.2
acetaldehyde
pH 8.0 and 25°C, NAD+
17.2
acetaldehyde
-
wild-type protein, steady state, pH 8.0, 25°C
42
acetaldehyde
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I195L mutant, steady state, pH 8.0, 25°C
4.63
acetyl-CoA
-
recombinant enzyme, pH 7.15, 30°C
11.33
acetyl-CoA
recombinant enzyme, pH 7.15, 30°C
14.81
acetyl-CoA
-
recombinant enzyme, pH 7.15, 30°C
7.02
butanoyl-CoA
-
recombinant enzyme, pH 7.15, 30°C
11.99
butanoyl-CoA
recombinant enzyme, pH 7.15, 30°C
25.38
butanoyl-CoA
-
recombinant enzyme, pH 7.15, 30°C
2.3
propionaldehyde
BphJ-TTHB246 complex, pH 8.0, 25°C
2.6
propionaldehyde
TTHB247-BphI complex, pH 8.0, 25°C
3.6
propionaldehyde
TTHB246-TTHB247 complex, pH 8.0, 25°C
8.4
propionaldehyde
single TTHB247, pH 8.0, 25°C
8.9
propionaldehyde
-
I195F mutant, steady state, pH 8.0, 25°C
16.3
propionaldehyde
BphJ-BphI complex, pH 8.0, 25°C
16.3
propionaldehyde
pH 8.0 and 25°C, NAD+
16.3
propionaldehyde
-
wild-type protein, steady state, pH 8.0, 25°C
46
propionaldehyde
-
I195L mutant, steady state, pH 8.0, 25°C
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0.3
Butyraldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
1.4
Isobutyraldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
405.2
NAD+
app. Km-value with acetaldehyde as substrate, pH 8.0 and 25°C
22.99
NADP+
app. Km-value with acetaldehyde as substrate, pH 8.0 and 25°C
0.076
pentaldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
0.14 - 1.31
propionaldehyde
0.14
acetaldehyde
BphJ-TTHB246 complex, pH 8.0, 25°C
0.23
acetaldehyde
TTHB246-TTHB247 complex, pH 8.0, 25°C
0.3
acetaldehyde
TTHB247-BphI complex, pH 8.0, 25°C
0.73
acetaldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
0.73
acetaldehyde
BphJ-BphI complex, pH 8.0, 25°C
1.35
acetaldehyde
single TTHB247, pH 8.0, 25°C
25
acetyl-CoA
-
recombinant enzyme, pH 7.15, 30°C
43
acetyl-CoA
-
recombinant enzyme, pH 7.15, 30°C
122
acetyl-CoA
recombinant enzyme, pH 7.15, 30°C
125
butanoyl-CoA
-
recombinant enzyme, pH 7.15, 30°C
167
butanoyl-CoA
recombinant enzyme, pH 7.15, 30°C
292
butanoyl-CoA
-
recombinant enzyme, pH 7.15, 30°C
0.14
propionaldehyde
BphJ-TTHB246 complex, pH 8.0, 25°C
0.22
propionaldehyde
TTHB246-TTHB247 complex, pH 8.0, 25°C
0.27
propionaldehyde
TTHB247-BphI complex, pH 8.0, 25°C
0.7
propionaldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
0.7
propionaldehyde
BphJ-BphI complex, pH 8.0, 25°C
1.31
propionaldehyde
single TTHB247, pH 8.0, 25°C
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17
with butanoyl-CoA, pH 7.15, 30°C
8.9
-
with butanoyl-CoA, pH 7.15, 30°C
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7.15
-
assay at
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30
-
assay at
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-
-
brenda
-
UniProt
brenda
-
UniProt
brenda
-
-
-
brenda
-
UniProt
brenda
-
UniProt
brenda
-
-
-
brenda
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metabolism
enzyme forms a bifunctional complex with EC 4.1.3.43 (BphI), 4-hydroxy-2-oxohexanoate aldolase and is part of the polychlorinated biphenyl degradation pathway
metabolism
-
enzyme is part of the BphI-BphJ-complex, an aldolase-dehydrogenase-complex from the polychlorinated biphenyl degradation pathway
metabolism
together with TTHB246, EC 4.1.3.43, the enzyme forms a bacterial aldolase-dehydrogenase complex catalyzing the last steps in the meta cleavage pathway of aromatic hydrocarbon degradation
metabolism
-
the oxygen sensitivity of CoA-acylating aldehyde dehydrogenase appears to be a key limiting factor for cyanobacteria to produce alcohols through the CoA-dependent route
metabolism
the oxygen sensitivity of CoA-acylating aldehyde dehydrogenase appears to be a key limiting factor for cyanobacteria to produce alcohols through the CoA-dependent route
metabolism
-
the oxygen sensitivity of CoA-acylating aldehyde dehydrogenase appears to be a key limiting factor for cyanobacteria to produce alcohols through the CoA-dependent route
-
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PDUP_CITFR
461
0
48671
Swiss-Prot
-
PDUP_SALTY
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
464
0
49046
Swiss-Prot
-
ACDH_THET8
Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
307
0
33115
Swiss-Prot
-
ACDH_MYCBO
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
303
0
32009
Swiss-Prot
-
ACDH_MYCBP
Mycobacterium bovis (strain BCG / Pasteur 1173P2)
303
0
32009
Swiss-Prot
-
ACDH_MYCBT
Mycobacterium bovis (strain BCG / Tokyo 172 / ATCC 35737 / TMC 1019)
303
0
32009
Swiss-Prot
-
ACDH_MYCTA
Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
303
0
32009
Swiss-Prot
-
ACDH4_PARXL
Paraburkholderia xenovorans (strain LB400)
304
0
32237
Swiss-Prot
-
ACDH_MYCTO
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
303
0
32009
Swiss-Prot
-
ACDH_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
303
0
32009
Swiss-Prot
-
A0A1A2X0F3_9MYCO
256
0
27228
TrEMBL
-
A0A1A2XR09_9MYCO
205
0
21664
TrEMBL
-
A0A1J5PFK0_9ZZZZ
299
0
31744
TrEMBL
other Location (Reliability: 1 )
A0A1J5RQA4_9ZZZZ
307
0
32580
TrEMBL
other Location (Reliability: 2 )
A0A841KZ92_9CLOT
464
0
50272
TrEMBL
-
A0A0B5QJH1_CLOBE
449
0
48889
TrEMBL
-
A0A1S8R1T1_CLOBE
472
0
51558
TrEMBL
-
A0A1A2QJ81_9MYCO
283
0
29991
TrEMBL
-
A0A7W6Y4A3_9HYPH
552
0
57765
TrEMBL
-
A0A2S8LPD7_9MYCO
151
0
16152
TrEMBL
-
A0A839W8V0_9ENTR
506
0
53475
TrEMBL
-
A0A6A4X8L2_PEDAC
477
0
50709
TrEMBL
-
A0A1B9D3D7_MYCMA
262
0
27925
TrEMBL
-
A0A7W9Y8X4_9HYPH
552
0
57644
TrEMBL
-
A0A841G9M4_9GAMM
467
0
49468
TrEMBL
-
Q716S8_CLOBE
468
0
51273
TrEMBL
-
A0A5N0GD83_9MYCO
130
0
13827
TrEMBL
-
A0A1S8QQ58_CLOBE
210
0
23456
TrEMBL
-
A0A1B9D0X7_MYCMA
262
0
27883
TrEMBL
-
A0A2S8LP70_9MYCO
151
0
16165
TrEMBL
-
A0A1A2XH46_9MYCO
209
0
22049
TrEMBL
-
A0A1A2WHJ1_9MYCO
256
0
27287
TrEMBL
-
A0A0E0UUX4_LISMM
Listeria monocytogenes serotype 4a (strain M7)
469
0
50309
TrEMBL
-
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137000
molecular mass of BphI-TTHB247 chimeric complex, determined by static light scattering
140000
native molecular mass of the purified BphI-BphJ-complex, estimated by gel filtration
142000
native molecular mass of TTHB246-TTHB247 complex, determined by gel filtration
144000
molecular mass of BphI-TTHB247 chimeric complex, determined by gel filtration
152000
native molecular mass of TTHB246-TTHB247 complex, determined by static light scattering
32000
SDS-PAGE, in agreement with the predicted molecular mass calculated from amino acid sequence
37000
BphI-BphJ-complex, alpha2beta2, 2 * 32000 BphJ, 2 * 37000 BphI, estimated by gel filtration
40000
native molecular mass of TTHB247, determined by gel filtration
33000
estimated by SDS-PAGE, in agreement with predicted molecular mass calculated from amino acid sequences
33000
native molecular mass of TTHB247, determined by static light scattering
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heterotetramer
BphI-BphJ-complex, alpha2beta2, 2 * 32000 BphJ, 2 * 37000 BphI, estimated by gel filtration
monomer
1 * 33000, SDS-PAGE, enzyme can form a stable heterotetrameric complex with TTHB246 in vitro, consisting of two aldolase and two dehydrogenase subunits
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I195F
-
created by site-specific mutagenesis, no significant reduction of channeling efficiency of the enzyme complex toward acetaldehyde or propionaldehyde
I195L
-
created by site-specific mutagenesis
additional information
-
design of a coenzyme A (CoA) dependent n-butanol biosynthesis pathway tailored to the metabolic physiology of the cyanobacterium Synechococcus elongatus PCC 7942 by incorporating an ATP driving force and a kinetically irreversible trap. Oxygen-sensitive CoA-acylating butyraldehyde dehydrogenase (Bldh) is exchanged for the oxygen-tolerant PduP from Salmonella enterica. Replacing Bldh with PduP in the n-butanol synthesis pathway results in n-butanol production to a cumulative titer of 404 mg/l with peak productivity of 51 mg/l per day, exceeding the base strain by 20fold. Anaerobic growth rescue of Escherichia coli strain JCL166 by overexpression of the Clostridium butanol pathway with different aldehyde dehydrogenases PduP
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50
half-life in complex with TTHB246 is 5.9 h
50
half-life of chimeric BphI-TTHB247 complex is 0.54 h for BphI activity and 2.47 for TTHB247 activity
50
half-life of single enzyme is 1.6 h
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the enzyme is oxygen-tolerant
the enzyme is oxygen-tolerant
-
742372
the enzyme is oxygen-tolerant
-
742372
the enzyme is oxygen-tolerant
742372
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purified enzyme can be stored at -80°C, without loss of activity for at least 12 months
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BphI and BphJ form a stable complex as they bind and coelute from Ni2+-NTA column, after purification N-terminal histidine tag of BphJ is proteolytically cleaved by thrombin digestion
-
BphI and BphJ form a stable complex as they bind and coelute from Ni2+-NTA column, although only BphJ has the histidine tag. After purification, the N-terminal histidine tag of BphJ is proteolytically cleaved by thrombin digestion
purified to homogeneity using Ni2+-NTA chromatography
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bphI and bphJ cloned into the plasmids pBTL4-T7 and pET28a
-
chimeric complexes of Burkholderia xenovorans and Thermus thermophilus enzymes, TTHB246-BphJ and BphI-TTHB247 created by coexpression of the relevant genes in Escherichia coli using separate expression plasmids
coexpression of bphI and bphJ in Escherichia coli using two compatible plasmids (pBTL4 and pET28a) yield soluble proteins
gene pduP, recombinant expression in Escherichia coli strain JCL166, strain JCL166 cannot grow anaerobically unless complemented by an exogenous fermentation pathway such as n-butanol biosynthesis. Recombinant coexpression of PduP with the enzymes of the n-butanol synthesis pathway in Synechococcus elongatus strain PCC 7942 results in autotrophic n-butanol production. PduP from Klebsiella pneumoniae produces more n-butanol than ethanol
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gene pduP, recombinant expression in Escherichia coli strain JCL166, strain JCL166 cannot grow anaerobically unless complemented by an exogenous fermentation pathway such as n-butanol biosynthesis. Recombinant coexpression of PduP with the enzymes of the n-butanol synthesis pathway in Synechococcus elongatus strain PCC 7942 results in autotrophic n-butanol production. PduP from Listeria monocytogenes produces more ethanol than n-butanol
gene pduP, recombinant expression in Escherichia coli strain JCL166, strain JCL166 cannot grow anaerobically unless complemented by an exogenous fermentation pathway such as n-butanol biosynthesis. Recombinant coexpression of PduP with the enzymes of the n-butanol synthesis pathway in Synechococcus elongatus strain PCC 7942 results in autotrophic n-butanol production. PduP from Salmonella enterica produces more ethanol than n-butanol
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separate expression of TTHB247 in recombinant Escherichia coli
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Baker, P.; Pan, D.; Carere, J.; Rossi, A.; Wang, W.; Seah, S.Y.K.
Characterization of an aldolase-dehydrogenase complex that exhibits substrate channeling in the polychlorinated biphenyls degradation pathway
Biochemistry
48
6551-6558
2009
Paraburkholderia xenovorans (Q79AF6)
brenda
Carere, J.; Baker, P.; Seah, S.Y.K.
Investigating the molecular determinants for substrate channeling in BphI-BphJ, an aldolase-dehydrogenase complex from the polychlorinated biphenyls degradation pathway
Biochemistry
50
8407-8416
2011
Paraburkholderia xenovorans
brenda
Baker, P.; Hillis, C.; Carere, J.; Seah, S.Y.K.
Protein-protein interactions and substrate channeling in orthologous and chimeric aldolase-dehydrogenase complexes
Biochemistry
51
1942-1952
2012
Thermus thermophilus (Q53WH9)
brenda
Lan, E.; Ro, S.; Liao, J.
Oxygen-tolerant coenzyme A-acylating aldehyde dehydrogenase facilitates efficient photosynthetic n-butanol biosynthesis in cyanobacteria
Energy Environ. Sci.
6
2672-2681
2013
Salmonella enterica, Klebsiella pneumoniae, Listeria monocytogenes (A0A0E0UUX4), Listeria monocytogenes M7 (A0A0E0UUX4)
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brenda
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