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Literature summary extracted from
- Monitoring conformational changes during the catalytic cycle of OpuAA, the ATPase subunit of the ABC transporter OpuA from Bacillus subtilis (2008), Biochem. J., 412, 233-244.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 7.6.2.9 | expressed in Escherichia coli, cysteine mutants generated and inserted into pBAD33 | Bacillus subtilis |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 7.5.2.1 | MalK crystal structure analysis in the semi-open, nucleotide-free, the open nucleotide-free, the ATP-bound, and the ADP-bound states | Escherichia coli |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 7.6.2.9 | F19W | mutant analyzed | Bacillus subtilis |
| 7.6.2.9 | G161C | single cysteine mutants generated by site-directed mutagenesis | Bacillus subtilis |
| 7.6.2.9 | S171C | single cysteine mutants generated by site-directed mutagenesis | Bacillus subtilis |
| 7.6.2.9 | S45C | single cysteine mutants generated by site-directed mutagenesis | Bacillus subtilis |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 7.6.2.9 | 0.6 | - |
ATP | wild-type, performed in 10 mM sodium phosphate, pH 7.5 and 1 M NaCl, monomeric form | Bacillus subtilis |  |
| 7.6.2.9 | 0.7 | - |
ATP | mutant S45C, performed in 10 mM sodium phosphate, pH 7.5 and 1 M NaCl, monomeric form | Bacillus subtilis | |
| 7.6.2.9 | 1.7 | - |
ATP | mutant F19W, performed in 10 mM sodium phosphate, pH 7.5 and 1 M NaCl, monomeric form | Bacillus subtilis | |
| 7.6.2.9 | 2.8 | - |
ATP | mutant G161C, performed in 10 mM sodium phosphate, pH 7.5 and 1 M NaCl, monomeric form | Bacillus subtilis | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.5.2.1 | ATP + H2O + maltose/out | Escherichia coli | - |
ADP + phosphate + maltose/in | - |
? | |
| 7.5.2.1 | additional information | Escherichia coli | MalK is the ABC-ATPase of the maltose importer of Escherichia coli. The MalK accessory domain interacts with at least two enzymes, MalT and IIA | ? | - |
? | |
| 7.6.2.9 | ATP + H2O | Bacillus subtilis | - |
ADP + phosphate | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 7.5.2.1 | Escherichia coli | P68187 | - |
- |
| 7.6.2.9 | Bacillus subtilis | P46920 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 7.6.2.9 | gel filtration | Bacillus subtilis |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 7.6.2.9 | additional information | - |
studies on architecture and potential roles of the C-terminal accessory domain in structural and functional protein regulation performed, conformational changes during the catalytic cycle of the ATPase unit of OpuA protein determined, single cysteine mutants generated, static and time-resolved FRET measurements applied, molecular modelling and structural analysis shown | Bacillus subtilis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.5.2.1 | ATP + H2O + maltose/out | - |
Escherichia coli | ADP + phosphate + maltose/in | - |
? | |
| 7.5.2.1 | additional information | MalK is the ABC-ATPase of the maltose importer of Escherichia coli. The MalK accessory domain interacts with at least two enzymes, MalT and IIA | Escherichia coli | ? | - |
? | |
| 7.6.2.9 | ATP + H2O | - |
Bacillus subtilis | ADP + phosphate | - |
? | |
| 7.6.2.9 | ATP + H2O | ATPase activity of monomeric OpuA protein measured in wild-type and single cysteine mutants, structural information on the architecture of the OpuA-ATPase by application of FRET techniques, C-terminal catalytic domain, helical domain and accessory domain analyzed | Bacillus subtilis | ADP + phosphate | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 7.5.2.1 | dimer | MalK structure comparison, the enzyme contains two cystathione beta-synthetase domains | Escherichia coli |
| 7.5.2.1 | More | MalK-derived homology model, overview | Escherichia coli |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 7.5.2.1 | MalK | - |
Escherichia coli |
| 7.5.2.1 | maltose importer | - |
Escherichia coli |
| 7.6.2.9 | OpuA | - |
Bacillus subtilis |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 7.6.2.9 | 22 | - |
assay at | Bacillus subtilis |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 7.6.2.9 | 20 | 24 | assay at | Bacillus subtilis |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 7.6.2.9 | 7.5 | - |
assay at | Bacillus subtilis |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.5.2.1 | ATP | structure of the nucleotide-binding domain of the maltose importer, comparison, overview | Escherichia coli | |
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Release 2023.1 (January 2023)
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