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Literature summary for 2.3.1.122 extracted from
- Specific ion influences on self-association of pyruvate dehydrogenase kinase isoform 2 (PDHK2), binding of PDHK2 to the L2 lipoyl domain, and effects of the lipoyl group-binding site inhibitor, Nov3r (2008), Biochemistry, 47, 2312-2324.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli as a His-tagged fusion protein | Mycobacterium avium |
| expressed in Escherichia coli as a His-tagged fusion protein | Mycobacterium leprae |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| L130S | leucine at position 130 of Mycobacterium leprae FbpA limits access of mycolate-containing glycolipid substrates to their binding site. Mutant L130S exhibits an enhanced mycosyltransferase activity compared to wild-type while the ability to transfer the unbranched acyl chain is unchanged. Km (substrate: short-chain trehalose monomycolate): 0.043 mM, sharply decreased compared to wild-type | Mycobacterium leprae |
| S130L | mutant S130L of Mycobacterium avium exhibits a reduced mycosyltransferase activity compared to wild-type | Mycobacterium avium |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.043 | - |
alpha,alpha-trehalose 6-monomycolate | mutant L130S, short-chain trehalose monomycolate is used as a substrate, Vmax: 4.27 nmol/min/nmol | Mycobacterium leprae |  |
| 0.459 | - |
alpha,alpha-trehalose 6-monomycolate | wild-type, short-chain trehalose monomycolate is used as a substrate, Vmax: 3.83 nmol/min/nmol | Mycobacterium leprae | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mycobacterium avium | - |
- |
- |
| Mycobacterium leprae | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| using Ni-NTA chromatography | Mycobacterium avium |
| using Ni-NTA chromatography | Mycobacterium leprae |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
compared to FbpA of Mycobacterium leprae activity of FbpA is strikingly enhanced in Mycobacterium avium | Mycobacterium avium |
| additional information | - |
compared to FbpA of Mycobacterium tuberculosis and Mycobacterium avium activity of FbpA is reduced in Mycobacterium leprae | Mycobacterium leprae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 alpha,alpha-trehalose 6-monomycolate | - |
Mycobacterium avium | alpha,alpha-trehalose 6,6'-dimycolate + alpha,alpha-trehalose | - |
? | |
| 2 alpha,alpha-trehalose 6-monomycolate | substrate contains alpha-branched long-chain fatty acids. Only tiny amounts of trehalose dimycolate are detected. It is shown that FbpA mycolyltransferase from Mycobacterium leprae retains the ability to transfer unbranched but not alpha-branched fatty acids | Mycobacterium leprae | alpha,alpha-trehalose 6,6'-dimycolate + alpha,alpha-trehalose | - |
? | |
| alpha,alpha-trehalose monomycolate + D-glucose | D-glucose is used as an alternative acceptor substrate. FbpA mycolyltransferase from Mycobacterium leprae shows only trace of glucose monomycolate is detected | Mycobacterium leprae | D-glucose monomycolate + alpha,alpha-trehalose | - |
? | |
| alpha,alpha-trehalose monomycolate + D-glucose | Mycobacterium tuberculosis and Mycobacterium avium, replace TDM with glucose monomycolate by borrowing host-derived glucose as an alternative substrate for the FbpA mycolyltransferase | Mycobacterium avium | D-glucose monomycolate + alpha,alpha-trehalose | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| FbpA mycolyltransferase | - |
Mycobacterium avium |
| FbpA mycolyltransferase | - |
Mycobacterium leprae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Mycobacterium avium |
| 37 | - |
assay at | Mycobacterium leprae |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Mycobacterium avium |
| 7.5 | - |
assay at | Mycobacterium leprae |
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Release 2023.1 (January 2023)
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