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

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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Entner Doudoroff pathway
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Pentose phosphate pathway
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Metabolic pathways
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Microbial metabolism in diverse environments
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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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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 + 2,6-dichlorophenolindophenol
D-glycerate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
D-glyceraldehyde + H2O + acceptor
D-glycerate + reduced acceptor
show the reaction diagram
D-glyceraldehyde + H2O + methyl viologen
D-glycerate + reduced methyl viologen
show the reaction diagram
D-glyceraldehyde-3-phosphate + H2O + methyl viologen
3-phospho-D-glycerate + reduced methyl viologen
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
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
show the reaction diagram
indolepyruvate + 2,6-dichlorophenolindophenol + H2O
? + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
F9VNL4; F9VNL6; F9VNL5;, Q96XN5; Q974U9; Q974V0;, Q96Y29; Q974U9; Q974V0;
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?
isobutyraldehyde + 2,6-dichlorophenolindophenol + H2O
isobutyrate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
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
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
molybdopterin cytosine dinucleotide
F9VNL4; F9VNL6; F9VNL5;, Q96XN5; Q974U9; Q974V0;, Q96Y29; Q974U9; Q974V0;
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molybdopterin guanine dinucleotide
contains 1 molybdopterin guanine dinucleotide per enzyme molecule
[2Fe-2S]-center
F9VNL4; F9VNL6; F9VNL5;, Q96XN5; Q974U9; Q974V0;, Q96Y29; Q974U9; Q974V0;
small subunit contains two [2Fe-2S] clusters
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
copper
F9VNL4; F9VNL6; F9VNL5;, Q96XN5; Q974U9; Q974V0;, Q96Y29; Q974U9; Q974V0;
0.3 nmol/mg protein; 0.56 nmol/mg protein; 0.76 nmol/mg protein
Molybdenum
F9VNL4; F9VNL6; F9VNL5;, Q96XN5; Q974U9; Q974V0;, Q96Y29; Q974U9; Q974V0;
2.9 nmol/mg protein; 4.46 nmol/mg protein; 5.5 nmol/mg protein
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.24 - 1.33
acetaldehyde
0.011 - 0.63
D-glyceraldehyde
0.0035 - 0.085
D-Glyceraldehyde-3-phosphate
0.09
DL-glyceraldehyde
80°C, pH 6.7
0.037 - 0.113
Indoleacetaldehyde
1.86
Indolepyruvate
F9VNL4; F9VNL6; F9VNL5;, Q96XN5; Q974U9; Q974V0;, Q96Y29; Q974U9; Q974V0;
cosubstrate methyl viologen, pH 7.0, 70°C
0.03
propionaldehyde
80°C, pH 6.7
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.23 - 3.38
acetaldehyde
0.72 - 50.5
D-glyceraldehyde
0.43 - 0.98
D-Glyceraldehyde-3-phosphate
2.77 - 3.58
Indoleacetaldehyde
11
Indolepyruvate
F9VNL4; F9VNL6; F9VNL5;, Q96XN5; Q974U9; Q974V0;, Q96Y29; Q974U9; Q974V0;
cosubstrate methyl viologen, pH 7.0, 70°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2
F9VNL4; F9VNL6; F9VNL5;, Q96XN5; Q974U9; Q974V0;, Q96Y29; Q974U9; Q974V0;
isoelectric focusing
6.3
F9VNL4; F9VNL6; F9VNL5;, Q96XN5; Q974U9; Q974V0;, Q96Y29; Q974U9; Q974V0;
isoelectric focusing
6.9
F9VNL4; F9VNL6; F9VNL5;, Q96XN5; Q974U9; Q974V0;, Q96Y29; Q974U9; Q974V0;
isoelectric focusing
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
19500
x * 80500 + x * 32000 + x * 19500, the exact subunit composition (alphabeta(x)gamma(y)) could not be determined, SDS-PAGE
20000
F9VNL4; F9VNL6; F9VNL5;, Q96XN5; Q974U9; Q974V0;, Q96Y29; Q974U9; Q974V0;
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21000
F9VNL4; F9VNL6; F9VNL5;, Q96XN5; Q974U9; Q974V0;, Q96Y29; Q974U9; Q974V0;
;
29000
F9VNL4; F9VNL6; F9VNL5;, Q96XN5; Q974U9; Q974V0;, Q96Y29; Q974U9; Q974V0;
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30000
F9VNL4; F9VNL6; F9VNL5;, Q96XN5; Q974U9; Q974V0;, Q96Y29; Q974U9; Q974V0;
;
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
F9VNL4; F9VNL6; F9VNL5;, Q96XN5; Q974U9; Q974V0;, Q96Y29; Q974U9; Q974V0;
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82000
F9VNL4; F9VNL6; F9VNL5;, Q96XN5; Q974U9; Q974V0;, Q96Y29; Q974U9; Q974V0;
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83000
F9VNL4; F9VNL6; F9VNL5;, Q96XN5; Q974U9; Q974V0;, Q96Y29; Q974U9; Q974V0;
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85000
F9VNL4; F9VNL6; F9VNL5;, Q96XN5; Q974U9; Q974V0;, Q96Y29; Q974U9; Q974V0;
gel filtration
200000
F9VNL4; F9VNL6; F9VNL5;, Q96XN5; Q974U9; Q974V0;, Q96Y29; Q974U9; Q974V0;
gel filtration
372000
F9VNL4; F9VNL6; F9VNL5;, Q96XN5; Q974U9; Q974V0;, Q96Y29; Q974U9; Q974V0;
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dodecamer
heterohexamer
heterotrimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
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
F9VNL4; F9VNL6; F9VNL5;, Q96XN5; Q974U9; Q974V0;, Q96Y29; Q974U9; Q974V0;
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
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
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
F9VNL4; F9VNL6; F9VNL5;, Q96XN5; Q974U9; Q974V0;, Q96Y29; Q974U9; Q974V0;