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Enzyme Nomenclature
Information on EC 1.2.99.8 - glyceraldehyde dehydrogenase (FAD-containing)
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The expected taxonomic range for this enzyme is: Archaea, Bacteria
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EC NUMBER 
COMMENTARY 
1.2.99.8
-
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RECOMMENDED NAME
GeneOntology No.
glyceraldehyde dehydrogenase (FAD-containing)
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-glyceraldehyde + H2O + acceptor = D-glycerate + reduced acceptor
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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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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
Q96XN5 i.e. gene product ST2484, Q974U9 i.e. gene product ST0562, Q974V0 i.e. gene product ST0561
Q96XN5, Q974U9, Q974V0
UniProt
Q96Y29 i.e. gene product ST2339, Q974U9 i.e. gene product ST0562, Q974V0 i.e. gene product ST0561
Q96Y29, Q974U9, Q974V0
UniProt
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
Q96XN5 i.e. gene product ST2484, Q974U9 i.e. gene product ST0562, Q974V0 i.e. gene product ST0561
Q96XN5, Q974U9, Q974V0
UniProt
Q96Y29 i.e. gene product ST2339, Q974U9 i.e. gene product ST0562, Q974V0 i.e. gene product ST0561
Q96Y29, Q974U9, Q974V0
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
function as a glyceraldehyde oxidoreductase in the course of the nonphosphorylative Entner-Doudoroff pathway
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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 SUBSTRATES
NATURAL PRODUCTS
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
Q4J6M3 AND Q4J6M6 AND Q4J6M5
function as a glyceraldehyde oxidoreductase in the course of the nonphosphorylative Entner-Doudoroff pathway
-
-
?
D-glyceraldehyde + H2O + acceptor
D-glycerate + reduced acceptor
Q4J6M3 AND Q4J6M6 AND Q4J6M5
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
0.3 nmol/mg protein; 0.56 nmol/mg protein; 0.76 nmol/mg protein
Iron
Molybdenum
2.9 nmol/mg protein; 4.46 nmol/mg protein; 5.5 nmol/mg protein
Iron
contains either one [4Fe-4S]-cluster or two [2Fe-2S]-clusters per molecule
Iron
10.5 nmol/mg protein; 18.6 nmol/mg protein; 26.2 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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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
present in the cytosol to at least 0.4% of the soluble protein
-
present in the cytosol to at least 0.4% of the soluble protein
-
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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
-
21000
;
29000
-
30000
;
32000
x * 80500 + x * 32000 + x * 19500, the exact subunit composition (alphabeta(x)gamma(y)) could not be determined, SDS-PAGE
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
200000
gel filtration
372000
gel filtration
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SUBUNITS
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; purified enzyme is dark red in color; purified enzyme is dark red in color
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LINKS TO OTHER DATABASES (specific for EC-Number 1.2.99.8)
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