1.2.99.8: glyceraldehyde dehydrogenase (FAD-containing)
This is an abbreviated version!
For detailed information about glyceraldehyde dehydrogenase (FAD-containing), go to the full flat file.
Word Map on EC 1.2.99.8
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1.2.99.8
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chaperonins
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hetero-oligomeric
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t-complex
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ring-shaped
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cryo-em
- 1.2.99.8
- chaperonins
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hetero-oligomeric
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t-complex
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ring-shaped
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cryo-em
Reaction
Synonyms
Gaor1, Gaor2, Gaor3, glyceraldehyde oxidoreductase, ST0561, ST0562, ST1781, ST1782, ST1783, ST2339, ST2484
ECTree
1.2.99.8 glyceraldehyde dehydrogenase (FAD-containing)Advanced search results
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results (Substrates Products
Substrates Products on EC 1.2.99.8 - glyceraldehyde dehydrogenase (FAD-containing)
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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
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?
indoleacetaldehyde + 2,6-dichlorophenolindophenol + H2O
indoleacetate + reduced 2,6-dichlorophenolindophenol
indolepyruvate + 2,6-dichlorophenolindophenol + H2O
? + reduced 2,6-dichlorophenolindophenol
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-
-
?
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
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-
?
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
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-
?
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
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-
?
acetaldehyde + 2,6-dichlorophenolindophenol + H2O
acetate + reduced 2,6-dichlorophenolindophenol
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-
?
acetaldehyde + 2,6-dichlorophenolindophenol + H2O
acetate + reduced 2,6-dichlorophenolindophenol
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-
-
?
D-glyceraldehyde + H2O + 2,6-dichlorophenolindophenol
D-glycerate + reduced 2,6-dichlorophenolindophenol
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-
-
?
D-glyceraldehyde + H2O + 2,6-dichlorophenolindophenol
D-glycerate + reduced 2,6-dichlorophenolindophenol
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-
?
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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-
?
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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?
D-glyceraldehyde + H2O + methyl viologen
D-glycerate + reduced methyl viologen
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?
D-glyceraldehyde + H2O + methyl viologen
D-glycerate + reduced methyl viologen
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?
D-glyceraldehyde-3-phosphate + H2O + methyl viologen
3-phospho-D-glycerate + reduced methyl viologen
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?
D-glyceraldehyde-3-phosphate + H2O + methyl viologen
3-phospho-D-glycerate + reduced methyl viologen
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?
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
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?
indoleacetaldehyde + 2,6-dichlorophenolindophenol + H2O
indoleacetate + reduced 2,6-dichlorophenolindophenol
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-
?
additional information
?
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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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-
?
additional information
?
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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
?
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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
-
-
?
