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Literature summary for 1.2.99.8 extracted from
- The strict molybdate-dependence of glucose-degradation by the thermoacidophile Sulfolobus acidocaldarius reveals the first crenarchaeotic molybdenum containing enzyme - an aldehyde oxidoreductase (1999), Eur. J. Biochem., 260, 540-548.
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.03 | - |
propionaldehyde | 80°C, pH 6.7 | Sulfolobus acidocaldarius |  |
| 0.09 | - |
DL-glyceraldehyde | 80°C, pH 6.7 | Sulfolobus acidocaldarius | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytosol | present in the cytosol to at least 0.4% of the soluble protein | Sulfolobus acidocaldarius | 5829 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Iron | contains either one [4Fe-4S]-cluster or two [2Fe-2S]-clusters per molecule | Sulfolobus acidocaldarius | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 19500 | - |
x * 80500 + x * 32000 + x * 19500, the exact subunit composition (alphabeta(x)gamma(y)) could not be determined, SDS-PAGE | Sulfolobus acidocaldarius |
| 32000 | - |
x * 80500 + x * 32000 + x * 19500, the exact subunit composition (alphabeta(x)gamma(y)) could not be determined, SDS-PAGE | Sulfolobus acidocaldarius |
| 80500 | - |
x * 80500 + x * 32000 + x * 19500, the exact subunit composition (alphabeta(x)gamma(y)) could not be determined, SDS-PAGE | Sulfolobus acidocaldarius |
| 177000 | - |
gel filtration | Sulfolobus acidocaldarius |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-glyceraldehyde + H2O + acceptor | Sulfolobus acidocaldarius | function as a glyceraldehyde oxidoreductase in the course of the nonphosphorylative Entner-Doudoroff pathway | D-glycerate + reduced acceptor | - |
? | |
| D-glyceraldehyde + H2O + acceptor | Sulfolobus acidocaldarius DSM 639 | function as a glyceraldehyde oxidoreductase in the course of the nonphosphorylative Entner-Doudoroff pathway | D-glycerate + reduced acceptor | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Sulfolobus acidocaldarius | Q4J6M3 AND Q4J6M6 AND Q4J6M5 | - |
- |
| Sulfolobus acidocaldarius DSM 639 | Q4J6M3 AND Q4J6M6 AND Q4J6M5 | - |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| phosphoprotein | phosphate content of 3.7 phosphates per molecule of protei | Sulfolobus acidocaldarius |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Sulfolobus acidocaldarius |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetaldehyde + 2,6-dichlorophenolindophenol + H2O | 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 | Sulfolobus acidocaldarius | acetate + reduced 2,6-dichlorophenolindophenol | - |
? | |
| acetaldehyde + 2,6-dichlorophenolindophenol + H2O | 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 | Sulfolobus acidocaldarius DSM 639 | acetate + reduced 2,6-dichlorophenolindophenol | - |
? | |
| D-glyceraldehyde + H2O + acceptor | function as a glyceraldehyde oxidoreductase in the course of the nonphosphorylative Entner-Doudoroff pathway | Sulfolobus acidocaldarius | D-glycerate + reduced acceptor | - |
? | |
| D-glyceraldehyde + H2O + acceptor | function as a glyceraldehyde oxidoreductase in the course of the nonphosphorylative Entner-Doudoroff pathway | Sulfolobus acidocaldarius DSM 639 | D-glycerate + reduced acceptor | - |
? | |
| DL-glyceraldehyde + 2,6-dichlorophenolindophenol + H2O | 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 | Sulfolobus acidocaldarius | glycerate + reduced 2,6-dichlorophenolindophenol | - |
? | |
| DL-glyceraldehyde + 2,6-dichlorophenolindophenol + H2O | 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 | Sulfolobus acidocaldarius DSM 639 | glycerate + reduced 2,6-dichlorophenolindophenol | - |
? | |
| formaldehyde + 2,6-dichlorophenolindophenol + H2O | 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 | Sulfolobus acidocaldarius | formate + reduced 2,6-dichlorophenolindophenol | - |
? | |
| formaldehyde + 2,6-dichlorophenolindophenol + H2O | 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 | Sulfolobus acidocaldarius DSM 639 | formate + reduced 2,6-dichlorophenolindophenol | - |
? | |
| glyceraldehyde-3-phosphate + 2,6-dichlorophenolindophenol + H2O | 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 | Sulfolobus acidocaldarius | 3-phospho-D-glycerate + reduced 2,6-dichlorophenolindophenol | - |
? | |
| isobutyraldehyde + 2,6-dichlorophenolindophenol + H2O | 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 | Sulfolobus acidocaldarius | isobutyrate + 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 | Sulfolobus acidocaldarius | ? | - |
? | |
| 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 | Sulfolobus acidocaldarius DSM 639 | ? | - |
? | |
| propionaldehyde + 2,6-dichlorophenolindophenol + H2O | 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 | Sulfolobus acidocaldarius | propionate + reduced 2,6-dichlorophenolindophenol | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 80500 + x * 32000 + x * 19500, the exact subunit composition (alphabeta(x)gamma(y)) could not be determined, SDS-PAGE | Sulfolobus acidocaldarius |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| glyceraldehyde oxidoreductase | - |
Sulfolobus acidocaldarius |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 65 | - |
assay at | Sulfolobus acidocaldarius |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 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 | Sulfolobus acidocaldarius |
| 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 | Sulfolobus acidocaldarius |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.7 | - |
at its pH-optimum (pH 6.7), close to the intracellular pH of Sulfolobus, the glyceraldehyde-oxidizing activity is predominant | Sulfolobus acidocaldarius |
| 7.5 | - |
enzyme preparation exhibits an increased catalytic activity towards glyceraldehyde-3-phosphate when shifting the pH from 7.5 to 6.7 | Sulfolobus acidocaldarius |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | contains 1 FAD per molecule | Sulfolobus acidocaldarius | |
| molybdopterin guanine dinucleotide | contains 1 molybdopterin guanine dinucleotide per enzyme molecule | Sulfolobus acidocaldarius | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | function as a glyceraldehyde oxidoreductase in the course of the nonphosphorylative Entner-Doudoroff pathway | Sulfolobus acidocaldarius |
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Release 2023.1 (January 2023)
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