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Information on EC 1.2.99.8 - glyceraldehyde dehydrogenase (FAD-containing)
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1.2.99.8 glyceraldehyde dehydrogenase (FAD-containing)IUBMB Comments
The enzyme from the archaeon Sulfolobus acidocaldarius catalyses the oxidation of D-glyceraldehyde in the nonphosphorylative Entner-Doudoroff pathway. With 2,6-dichlorophenolindophenol as artificial electron acceptor, the enzyme shows a broad substrate range, but is most active with D-glyceraldehyde. It is not known which acceptor is utilized in vivo. The iron-sulfur protein contains FAD and molybdopterin guanine dinucleotide.
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The expected taxonomic range for this enzyme is: Archaea, Bacteria
Synonyms
gaor2, glyceraldehyde oxidoreductase, st1781, gaor1, gaor3, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Gaor1
Gaor2
Gaor3
glyceraldehyde oxidoreductase
ST0561
ST0562
ST1781
ST1782
ST1783
ST2339
ST2484
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-glyceraldehyde + H2O + acceptor = D-glycerate + reduced acceptor
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
D-glyceraldehyde:acceptor oxidoreductase (FAD-containing)
The enzyme from the archaeon Sulfolobus acidocaldarius catalyses the oxidation of D-glyceraldehyde in the nonphosphorylative Entner-Doudoroff pathway. With 2,6-dichlorophenolindophenol as artificial electron acceptor, the enzyme shows a broad substrate range, but is most active with D-glyceraldehyde. It is not known which acceptor is utilized in vivo. The iron-sulfur protein contains FAD and molybdopterin guanine dinucleotide.
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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
acetaldehyde + 2,6-dichlorophenolindophenol + H2O
acetate + reduced 2,6-dichlorophenolindophenol
D-glyceraldehyde + H2O + 2,6-dichlorophenolindophenol
D-glycerate + reduced 2,6-dichlorophenolindophenol
D-glyceraldehyde-3-phosphate + H2O + methyl viologen
3-phospho-D-glycerate + reduced methyl viologen
DL-glyceraldehyde + 2,6-dichlorophenolindophenol + H2O
glycerate + reduced 2,6-dichlorophenolindophenol
formaldehyde + 2,6-dichlorophenolindophenol + H2O
formate + reduced 2,6-dichlorophenolindophenol
glyceraldehyde-3-phosphate + 2,6-dichlorophenolindophenol + H2O
3-phospho-D-glycerate + reduced 2,6-dichlorophenolindophenol
none of the tested electron acceptors (Sulfolobus ferredoxin, cytochrome c, NAD+, NADP+, benzoquinones, naphthoquinones) supports aldehyde oxidation as efficiently as 2,6-dichlorophenolindophenol. At pH 7.5, the enzyme exhibits activity preferentially towards the aliphatic aldehydes formaldehyde, acetaldehyde and propionaldehyde. At pH 6.7, supposed to be close to the intracellular pH of Sulfolobus, glyceraldehyde is the predominant substrate
-
?
indoleacetaldehyde + 2,6-dichlorophenolindophenol + H2O
indoleacetate + reduced 2,6-dichlorophenolindophenol
indolepyruvate + 2,6-dichlorophenolindophenol + H2O
? + reduced 2,6-dichlorophenolindophenol
-
-
?
isobutyraldehyde + 2,6-dichlorophenolindophenol + H2O
isobutyrate + reduced 2,6-dichlorophenolindophenol
none of the tested electron acceptors (Sulfolobus ferredoxin, cytochrome c, NAD+, NADP+, benzoquinones, naphthoquinones) supports aldehyde oxidation as efficiently as 2,6-dichlorophenolindophenol. At pH 7.5, the enzyme exhibits activity preferentially towards the aliphatic aldehydes formaldehyde, acetaldehyde and propionaldehyde. At pH 6.7, supposed to be close to the intracellular pH of Sulfolobus, glyceraldehyde is the predominant substrate
-
?
propionaldehyde + 2,6-dichlorophenolindophenol + H2O
propionate + reduced 2,6-dichlorophenolindophenol
none of the tested electron acceptors (Sulfolobus ferredoxin, cytochrome c, NAD+, NADP+, benzoquinones, naphthoquinones) supports aldehyde oxidation as efficiently as 2,6-dichlorophenolindophenol. At pH 7.5, the enzyme exhibited activity preferentially towards the aliphatic aldehydes formaldehyde, acetaldehyde and propionaldehyde. At pH 6.7, supposed to be close to the intracellular pH of Sulfolobus, glyceraldehyde is the predominant substrate
-
?
acetaldehyde + 2,6-dichlorophenolindophenol + H2O
acetate + reduced 2,6-dichlorophenolindophenol
none of the tested electron acceptors (Sulfolobus ferredoxin, cytochrome c, NAD+, NADP+, benzoquinones, naphthoquinones) supports aldehyde oxidation as efficiently as 2,6-dichlorophenolindophenol. At pH 7.5, the enzyme exhibited activity preferentially towards the aliphatic aldehydes formaldehyde, acetaldehyde and propionaldehyde. At pH 6.7, supposed to be close to the intracellular pH of Sulfolobus, glyceraldehyde is the predominant substrate
-
?
acetaldehyde + 2,6-dichlorophenolindophenol + H2O
acetate + reduced 2,6-dichlorophenolindophenol
none of the tested electron acceptors (Sulfolobus ferredoxin, cytochrome c, NAD+, NADP+, benzoquinones, naphthoquinones) supports aldehyde oxidation as efficiently as 2,6-dichlorophenolindophenol. At pH 7.5, the enzyme exhibited activity preferentially towards the aliphatic aldehydes formaldehyde, acetaldehyde and propionaldehyde. At pH 6.7, supposed to be close to the intracellular pH of Sulfolobus, glyceraldehyde is the predominant substrate
-
?
acetaldehyde + 2,6-dichlorophenolindophenol + H2O
acetate + reduced 2,6-dichlorophenolindophenol
-
-
?
acetaldehyde + 2,6-dichlorophenolindophenol + H2O
acetate + reduced 2,6-dichlorophenolindophenol
-
-
?
D-glyceraldehyde + H2O + 2,6-dichlorophenolindophenol
D-glycerate + reduced 2,6-dichlorophenolindophenol
-
-
?
D-glyceraldehyde + H2O + 2,6-dichlorophenolindophenol
D-glycerate + reduced 2,6-dichlorophenolindophenol
-
-
?
D-glyceraldehyde + H2O + acceptor
D-glycerate + reduced acceptor
function as a glyceraldehyde oxidoreductase in the course of the nonphosphorylative Entner-Doudoroff pathway
-
?
D-glyceraldehyde + H2O + acceptor
D-glycerate + reduced acceptor
function as a glyceraldehyde oxidoreductase in the course of the nonphosphorylative Entner-Doudoroff pathway
-
?
D-glyceraldehyde + H2O + methyl viologen
D-glycerate + reduced methyl viologen
-
-
?
D-glyceraldehyde + H2O + methyl viologen
D-glycerate + reduced methyl viologen
-
-
?
D-glyceraldehyde-3-phosphate + H2O + methyl viologen
3-phospho-D-glycerate + reduced methyl viologen
-
-
?
D-glyceraldehyde-3-phosphate + H2O + methyl viologen
3-phospho-D-glycerate + reduced methyl viologen
-
-
?
DL-glyceraldehyde + 2,6-dichlorophenolindophenol + H2O
glycerate + reduced 2,6-dichlorophenolindophenol
none of the tested electron acceptors (Sulfolobus ferredoxin, cytochrome c, NAD+, NADP+, benzoquinones, naphthoquinones) supports aldehyde oxidation as efficiently as 2,6-dichlorophenolindophenol. At pH 7.5, the enzyme exhibits activity preferentially towards the aliphatic aldehydes formaldehyde, acetaldehyde and propionaldehyde. At pH 6.7, supposed to be close to the intracellular pH of Sulfolobus, glyceraldehyde is the predominant substrate
-
?
DL-glyceraldehyde + 2,6-dichlorophenolindophenol + H2O
glycerate + reduced 2,6-dichlorophenolindophenol
none of the tested electron acceptors (Sulfolobus ferredoxin, cytochrome c, NAD+, NADP+, benzoquinones, naphthoquinones) supports aldehyde oxidation as efficiently as 2,6-dichlorophenolindophenol. At pH 7.5, the enzyme exhibits activity preferentially towards the aliphatic aldehydes formaldehyde, acetaldehyde and propionaldehyde. At pH 6.7, supposed to be close to the intracellular pH of Sulfolobus, glyceraldehyde is the predominant substrate
-
?
formaldehyde + 2,6-dichlorophenolindophenol + H2O
formate + reduced 2,6-dichlorophenolindophenol
none of the tested electron acceptors (Sulfolobus ferredoxin, cytochrome c, NAD+, NADP+, benzoquinones, naphthoquinones) supports aldehyde oxidation as efficiently as 2,6-dichlorophenolindophenol. At pH 7.5, the enzyme exhibits activity preferentially towards the aliphatic aldehydes formaldehyde, acetaldehyde and propionaldehyde. At pH 6.7, supposed to be close to the intracellular pH of Sulfolobus, glyceraldehyde is the predominant substrate
-
?
formaldehyde + 2,6-dichlorophenolindophenol + H2O
formate + reduced 2,6-dichlorophenolindophenol
none of the tested electron acceptors (Sulfolobus ferredoxin, cytochrome c, NAD+, NADP+, benzoquinones, naphthoquinones) supports aldehyde oxidation as efficiently as 2,6-dichlorophenolindophenol. At pH 7.5, the enzyme exhibits activity preferentially towards the aliphatic aldehydes formaldehyde, acetaldehyde and propionaldehyde. At pH 6.7, supposed to be close to the intracellular pH of Sulfolobus, glyceraldehyde is the predominant substrate
-
?
indoleacetaldehyde + 2,6-dichlorophenolindophenol + H2O
indoleacetate + reduced 2,6-dichlorophenolindophenol
-
-
?
indoleacetaldehyde + 2,6-dichlorophenolindophenol + H2O
indoleacetate + reduced 2,6-dichlorophenolindophenol
-
-
?
additional information
?
-
no activity with D-glucose. None of the tested electron acceptors (Sulfolobus ferredoxin, cytochrome c, NAD+, NADP+, benzoquinones, naphthoquinones) supports aldehyde oxidation as efficiently as 2,6-dichlorophenolindophenol
-
?
additional information
?
-
-
no activity with D-glucose. None of the tested electron acceptors (Sulfolobus ferredoxin, cytochrome c, NAD+, NADP+, benzoquinones, naphthoquinones) supports aldehyde oxidation as efficiently as 2,6-dichlorophenolindophenol
-
?
additional information
?
-
no activity with D-glucose. None of the tested electron acceptors (Sulfolobus ferredoxin, cytochrome c, NAD+, NADP+, benzoquinones, naphthoquinones) supports aldehyde oxidation as efficiently as 2,6-dichlorophenolindophenol
-
?
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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
D-glyceraldehyde + H2O + acceptor
D-glycerate + reduced acceptor
function as a glyceraldehyde oxidoreductase in the course of the nonphosphorylative Entner-Doudoroff pathway
-
-
?
D-glyceraldehyde + H2O + acceptor
D-glycerate + reduced acceptor
function as a glyceraldehyde oxidoreductase in the course of the nonphosphorylative Entner-Doudoroff pathway
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
molybdopterin cytosine dinucleotide
-
molybdopterin guanine dinucleotide
contains 1 molybdopterin guanine dinucleotide per enzyme molecule
[2Fe-2S]-center
small subunit contains two [2Fe-2S] clusters
FAD
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
copper
Iron
Molybdenum
copper
0.3 nmol/mg protein
copper
0.56 nmol/mg protein
copper
0.76 nmol/mg protein
Iron
contains either one [4Fe-4S]-cluster or two [2Fe-2S]-clusters per molecule
Iron
10.5 nmol/mg protein
Iron
18.6 nmol/mg protein
Iron
26.2 nmol/mg protein
Molybdenum
2.9 nmol/mg protein
Molybdenum
4.46 nmol/mg protein
Molybdenum
5.5 nmol/mg protein
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.86
Indolepyruvate
cosubstrate methyl viologen, pH 7.0, 70°C
0.24
acetaldehyde
cosubstrate methyl viologen, pH 7.0, 70°C
1.33
acetaldehyde
cosubstrate methyl viologen, pH 7.0, 70°C
0.011
D-glyceraldehyde
cosubstrate 2,6-dichlorophenolindophenol, pH 7.0, 70°C
0.018
D-glyceraldehyde
cosubstrate methyl viologen, pH 7.0, 70°C
0.03
D-glyceraldehyde
cosubstrate 2,6-dichlorophenolindophenol, pH 7.0, 70°C
0.091
D-glyceraldehyde
cosubstrate methyl viologen, pH 7.0, 70°C
0.138
D-glyceraldehyde
cosubstrate 2,6-dichlorophenolindophenol, pH 7.0, 70°C
0.63
D-glyceraldehyde
cosubstrate methyl viologen, pH 7.0, 70°C
0.0035
D-Glyceraldehyde-3-phosphate
cosubstrate methyl viologen, pH 7.0, 70°C
0.012
D-Glyceraldehyde-3-phosphate
cosubstrate methyl viologen, pH 7.0, 70°C
0.085
D-Glyceraldehyde-3-phosphate
cosubstrate methyl viologen, pH 7.0, 70°C
0.037
Indoleacetaldehyde
cosubstrate methyl viologen, pH 7.0, 70°C
0.092
Indoleacetaldehyde
cosubstrate methyl viologen, pH 7.0, 70°C
0.113
Indoleacetaldehyde
cosubstrate methyl viologen, pH 7.0, 70°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11
Indolepyruvate
cosubstrate methyl viologen, pH 7.0, 70°C
3.23
acetaldehyde
cosubstrate methyl viologen, pH 7.0, 70°C
3.38
acetaldehyde
cosubstrate methyl viologen, pH 7.0, 70°C
0.72
D-glyceraldehyde
cosubstrate methyl viologen, pH 7.0, 70°C
3.58
D-glyceraldehyde
cosubstrate 2,6-dichlorophenolindophenol, pH 7.0, 70°C
3.78
D-glyceraldehyde
cosubstrate 2,6-dichlorophenolindophenol, pH 7.0, 70°C
5.23
D-glyceraldehyde
cosubstrate methyl viologen, pH 7.0, 70°C
11.2
D-glyceraldehyde
cosubstrate methyl viologen, pH 7.0, 70°C
50.5
D-glyceraldehyde
cosubstrate 2,6-dichlorophenolindophenol, pH 7.0, 70°C
0.43
D-Glyceraldehyde-3-phosphate
cosubstrate methyl viologen, pH 7.0, 70°C
0.65
D-Glyceraldehyde-3-phosphate
cosubstrate methyl viologen, pH 7.0, 70°C
0.98
D-Glyceraldehyde-3-phosphate
cosubstrate methyl viologen, pH 7.0, 70°C
2.77
Indoleacetaldehyde
cosubstrate methyl viologen, pH 7.0, 70°C
3.46
Indoleacetaldehyde
cosubstrate methyl viologen, pH 7.0, 70°C
3.58
Indoleacetaldehyde
cosubstrate methyl viologen, pH 7.0, 70°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.7
at its pH-optimum (pH 6.7), close to the intracellular pH of Sulfolobus, the glyceraldehyde-oxidizing activity is predominant
7.5
enzyme preparation exhibits an increased catalytic activity towards glyceraldehyde-3-phosphate when shifting the pH from 7.5 to 6.7
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.2
isoelectric focusing
6.3
isoelectric focusing
6.9
isoelectric focusing
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
F9VNL4 i.e. gene product ST1781, F9VNL6 i.e. gene product ST1783, F9VNL5 i.e. gene product ST1782, cf. EC 1.2.3.7
UniProt
brenda
Q96XN5 i.e. gene product ST2484, Q974U9 i.e. gene product ST0562, Q974V0 i.e. gene product ST0561
Q96XN5; Q974U9; Q974V0
UniProt
brenda
Q96Y29 i.e. gene product ST2339, Q974U9 i.e. gene product ST0562, Q974V0 i.e. gene product ST0561
Q96Y29; Q974U9; Q974V0
UniProt
brenda
F9VNL4 i.e. gene product ST1781, F9VNL6 i.e. gene product ST1783, F9VNL5 i.e. gene product ST1782, cf. EC 1.2.3.7
UniProt
brenda
Q96XN5 i.e. gene product ST2484, Q974U9 i.e. gene product ST0562, Q974V0 i.e. gene product ST0561
Q96XN5; Q974U9; Q974V0
UniProt
brenda
Q96Y29 i.e. gene product ST2339, Q974U9 i.e. gene product ST0562, Q974V0 i.e. gene product ST0561
Q96Y29; Q974U9; Q974V0
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
present in the cytosol to at least 0.4% of the soluble protein
brenda
-
present in the cytosol to at least 0.4% of the soluble protein
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
function as a glyceraldehyde oxidoreductase in the course of the nonphosphorylative Entner-Doudoroff pathway
physiological function
-
function as a glyceraldehyde oxidoreductase in the course of the nonphosphorylative Entner-Doudoroff pathway
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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). CUTA_SULAC
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
748
0
82572
Swiss-Prot
-
CUTB_SULAC
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
281
0
30863
Swiss-Prot
-
CUTC_SULAC
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
163
0
17856
Swiss-Prot
-
A0A1Q9NDK4_HEILC
Heimdallarchaeota archaeon (strain LC_2)
483
0
53852
TrEMBL
-
A0A1Q9ND78_9ARCH
478
0
53998
TrEMBL
-
A0A0J8DD11_CLOCY
159
0
17350
TrEMBL
-
A0A1W6VP38_GEOTD
278
0
30807
TrEMBL
-
A0A151AAZ0_9EURY
159
0
17292
TrEMBL
-
A0A484HE52_9DELT
161
0
17258
TrEMBL
-
A0A1Q9ND68_9ARCH
278
0
31364
TrEMBL
-
A0A445N0F7_9DELT
uncultured Desulfobacterium sp
162
0
17471
TrEMBL
-
A0A0J8DCW0_CLOCY
158
0
17228
TrEMBL
-
A0A564Q9Z1_9EURY
274
0
30475
TrEMBL
-
A0A151AB57_9EURY
817
0
88716
TrEMBL
-
A0A151AAU1_9EURY
168
0
17946
TrEMBL
-
A0A151ABN8_9EURY
290
0
30607
TrEMBL
-
A0A1Q9NT51_HEILC
Heimdallarchaeota archaeon (strain LC_2)
274
0
31492
TrEMBL
-
A0A0H3IZH6_CLOPA
287
0
32283
TrEMBL
-
A0A151AAR3_9EURY
802
0
86402
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
19500
x * 80500 + x * 32000 + x * 19500, the exact subunit composition (alphabeta(x)gamma(y)) could not be determined, SDS-PAGE
20000
-
200000
gel filtration
21000
-
29000
-
30000
-
32000
x * 80500 + x * 32000 + x * 19500, the exact subunit composition (alphabeta(x)gamma(y)) could not be determined, SDS-PAGE
372000
gel filtration
80500
x * 80500 + x * 32000 + x * 19500, the exact subunit composition (alphabeta(x)gamma(y)) could not be determined, SDS-PAGE
81000
-
82000
-
83000
-
85000
gel filtration
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dodecamer
heterohexamer
heterotrimer
?
x * 80500 + x * 32000 + x * 19500, the exact subunit composition (alphabeta(x)gamma(y)) could not be determined, SDS-PAGE
?
-
x * 80500 + x * 32000 + x * 19500, the exact subunit composition (alphabeta(x)gamma(y)) could not be determined, SDS-PAGE
dodecamer
4 * 83000, gene product ST1781, plus 4 * 29000, gene product ST1783, plus 4 * 20000, gene product ST1782. Isoform Gaor1 is a tetramer of the gene products ST1781/ST1783/ST1782 hetero-trimer
dodecamer
-
4 * 83000, gene product ST1781, plus 4 * 29000, gene product ST1783, plus 4 * 20000, gene product ST1782. Isoform Gaor1 is a tetramer of the gene products ST1781/ST1783/ST1782 hetero-trimer
heterohexamer
2 * 81000, gene product ST2339, plus 2 * 30000, gene product ST0562, plus 2 * 21000, gene product ST0561. Isoform Gaor1 is a dimer of the gene products ST1781/ST1783/ST1782 heterotrimer
heterohexamer
-
2 * 81000, gene product ST2339, plus 2 * 30000, gene product ST0562, plus 2 * 21000, gene product ST0561. Isoform Gaor1 is a dimer of the gene products ST1781/ST1783/ST1782 heterotrimer
heterotrimer
1 * 82000, gene product ST2484, plus 1 * 30000, gene product ST0562, plus 1 * 21000, gene product ST0561
heterotrimer
-
1 * 82000, gene product ST2484, plus 1 * 30000, gene product ST0562, plus 1 * 21000, gene product ST0561
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
phosphate content of 3.7 phosphates per molecule of protei
phosphoprotein
-
phosphate content of 3.7 phosphates per molecule of protei
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 2.2 A resolution. The asymmetric unit contains one hetero-trimer, one Mo-PCD (large subunit), one FAD (medium subunit), two [2Fe-2S] clusters (designated as I and II, small subunit), and solvent molecules
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
92
apparent melting temperature, in association with other proteins the enzyme must be even more stable since it survived the prolonged heat treatment during the purification procedure
95
heating at 95°C results in total dissociation of the subunits, whereas heating at 56°C leads to the dissociation of the beta (32 kDa) subunit, only
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
purified enzyme is dark red in color
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kardinahl, S.; Schmidt, C.L.; Hansen, T.; Anemueller, S.; Petersen, A.; Schaefer, G.
The strict molybdate-dependence of glucose-degradation by the thermoacidophile Sulfolobus acidocaldarius reveals the first crenarchaeotic molybdenum containing enzyme - an aldehyde oxidoreductase
Eur. J. Biochem.
260
540-548
1999
Sulfolobus acidocaldarius (Q4J6M3 AND Q4J6M6 AND Q4J6M5
), Sulfolobus acidocaldarius, Sulfolobus acidocaldarius DSM 639 (Q4J6M3 AND Q4J6M6 AND Q4J6M5
)
brenda
Wakagi, T.; Nishimasu, H.; Miyake, M.; Fushinobu, S.
Archaeal Mo-containing glyceraldehyde oxidoreductase isozymes exhibit diverse substrate specificities through unique subunit assemblies
PLoS ONE
11
e0147333
2016
Sulfurisphaera tokodaii (F9VNL4 and F9VNL6 and F9VNL5), Sulfurisphaera tokodaii (Q96XN5 and Q974U9 and Q974V0), Sulfurisphaera tokodaii (Q96Y29 and Q974U9 and Q974V0), Sulfurisphaera tokodaii, Sulfurisphaera tokodaii DSM 16993 (F9VNL4 and F9VNL6 and F9VNL5), Sulfurisphaera tokodaii DSM 16993 (Q96XN5 and Q974U9 and Q974V0), Sulfurisphaera tokodaii DSM 16993 (Q96Y29 and Q974U9 and Q974V0)
brenda
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