Information on EC 1.2.99.8 - glyceraldehyde dehydrogenase (FAD-containing)

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The expected taxonomic range for this enzyme is: Sulfolobus acidocaldarius

EC NUMBER
COMMENTARY hide
1.2.99.8
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RECOMMENDED NAME
GeneOntology No.
glyceraldehyde dehydrogenase (FAD-containing)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-glyceraldehyde + H2O + acceptor = D-glycerate + reduced acceptor
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Entner-Doudoroff pathway II (non-phosphorylative)
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Metabolic pathways
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Microbial metabolism in diverse environments
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Pentose phosphate pathway
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Entner Doudoroff pathway
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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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Q4J6M3 AND Q4J6M6 AND Q4J6M5
SwissProt
Manually annotated by BRENDA team
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Q4J6M3 AND Q4J6M6 AND Q4J6M5
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
Q4J6M3 AND Q4J6M6 AND Q4J6M5
function as a glyceraldehyde oxidoreductase in the course of the nonphosphorylative Entner-Doudoroff pathway
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetaldehyde + 2,6-dichlorophenolindophenol + H2O
acetate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
D-glyceraldehyde + H2O + acceptor
D-glycerate + reduced acceptor
show the reaction diagram
DL-glyceraldehyde + 2,6-dichlorophenolindophenol + H2O
glycerate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
formaldehyde + 2,6-dichlorophenolindophenol + H2O
formate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
glyceraldehyde-3-phosphate + 2,6-dichlorophenolindophenol + H2O
3-phospho-D-glycerate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
Q4J6M3 AND Q4J6M6 AND Q4J6M5
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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?
isobutyraldehyde + 2,6-dichlorophenolindophenol + H2O
isobutyrate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
Q4J6M3 AND Q4J6M6 AND Q4J6M5
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
show the reaction diagram
Q4J6M3 AND Q4J6M6 AND Q4J6M5
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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?
additional information
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-glyceraldehyde + H2O + acceptor
D-glycerate + reduced acceptor
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
Q4J6M3 AND Q4J6M6 AND Q4J6M5
contains 1 FAD per molecule
molybdopterin guanine dinucleotide
Q4J6M3 AND Q4J6M6 AND Q4J6M5
contains 1 molybdopterin guanine dinucleotide per enzyme molecule
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
Q4J6M3 AND Q4J6M6 AND Q4J6M5
contains either one [4Fe-4S]-cluster or two [2Fe-2S]-clusters per molecule
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.09
DL-glyceraldehyde
Q4J6M3 AND Q4J6M6 AND Q4J6M5
80°C, pH 6.7
0.03
propionaldehyde
Q4J6M3 AND Q4J6M6 AND Q4J6M5
80°C, pH 6.7
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.7
Q4J6M3 AND Q4J6M6 AND Q4J6M5
at its pH-optimum (pH 6.7), close to the intracellular pH of Sulfolobus, the glyceraldehyde-oxidizing activity is predominant
7.5
Q4J6M3 AND Q4J6M6 AND Q4J6M5
enzyme preparation exhibits an increased catalytic activity towards glyceraldehyde-3-phosphate when shifting the pH from 7.5 to 6.7
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
Q4J6M3 AND Q4J6M6 AND Q4J6M5
assay at
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
19500
Q4J6M3 AND Q4J6M6 AND Q4J6M5
x * 80500 + x * 32000 + x * 19500, the exact subunit composition (alphabeta(x)gamma(y)) could not be determined, SDS-PAGE
32000
Q4J6M3 AND Q4J6M6 AND Q4J6M5
x * 80500 + x * 32000 + x * 19500, the exact subunit composition (alphabeta(x)gamma(y)) could not be determined, SDS-PAGE
80500
Q4J6M3 AND Q4J6M6 AND Q4J6M5
x * 80500 + x * 32000 + x * 19500, the exact subunit composition (alphabeta(x)gamma(y)) could not be determined, SDS-PAGE
177000
Q4J6M3 AND Q4J6M6 AND Q4J6M5
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
92
Q4J6M3 AND Q4J6M6 AND Q4J6M5
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
Q4J6M3 AND Q4J6M6 AND Q4J6M5
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
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
-
Q4J6M3 AND Q4J6M6 AND Q4J6M5