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Literature summary for 2.3.1.122 extracted from
- Mycolyltransferase-mediated glycolipid exchange in mycobacteria (2008), J. Biol. Chem., 283, 28835-28841.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed as a His-tagged fusion protein | Mycobacterium avium |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 33000 | - |
SDS-PAGE, detection of a fusion protein consiting of a His-tag and the mature Ag85A protein | Mycobacterium avium |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mycobacterium avium | B0I1V1 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| using Ni-NTA chromatography | Mycobacterium avium |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 alpha,alpha-trehalose 6-monomycolate | addition of glucose to this reaction condition results in decreased TDM production in a dose-dependent manner, which is associated with an increase in glucose monomycolate | Mycobacterium avium | alpha,alpha-trehalose 6,6'-dimycolate + alpha,alpha-trehalose | - |
? |  |
| alpha,alpha-trehalose monomycolate + D-glucose | trehalose dimycolate production decreases in a dose-dependent manner when glucose is added to the medium. It is hypothesized that trehalose monomycolate and glucose compete for access to the acceptor site of the Ag85A, and the enzyme preferentially catalyzes biosynthesis of glucose monomycolate, rather than trehalose dimycolate, when glucose is readily available | Mycobacterium avium | D-glucose monomycolate + alpha,alpha-trehalose | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Ag85A | - |
Mycobacterium avium |
| antigen 85A | - |
Mycobacterium avium |
| mycolyltransferase | - |
Mycobacterium avium |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Mycobacterium avium |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.4 | - |
assay at | Mycobacterium avium |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | glucose causes Mycobacterium avium to down-regulate trehalose dimycolate expression while up-regulating glucose monomycolate. In vitro, the mechanism of reciprocal regulation of trehalose dimycolate and glucose monomycolate involves competitive substrate selection by antigen 85A. The switch from trehalose dimycolate to glucose monomycolate biosynthesis occurs near the physiological concentration of glucose present in mammalian hosts. Furthermore, it is demonstrated that glucose monomycolate is produced in vivo by mcobacteria in mouse lung | Mycobacterium avium |
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Release 2023.1 (January 2023)
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