2.3.1.122: trehalose O-mycolyltransferase

This is an abbreviated version!
For detailed information about trehalose O-mycolyltransferase, go to the full flat file.

Word Map on EC 2.3.1.122

2.3.1.122

tuberculosis

mycobacterium

bovis

esat-6

antigen-specific

ifn-gamma

bacille

ankara

prime-boost

mva85a

immunodominant

mycolylation

bcg-vaccinated

mycolic

tuberculin

booster

polyfunctional

aerosol

bcg-primed

calmette-guerin

elispot

drug development

th1-type

fibronectin-binding

bcg-induced

medicine

tuberculosis-infected

biotechnology

dimycolate

post-vaccination

ifn-gamma-producing

Reaction

2 alpha,alpha-trehalose 6-mycolate =

Synonyms

Ag85A, ag85C, alpha,alpha'-trehalose 6-monomycolate:alpha,alpha'-trehalose mycolyltransferase, antigen 85A, antigen 85C, cg0413, CMT1, corynomycoloyl transferase C, FbpA mycolyltransferase, mycoloyl transferase, mycolyl-transferase Ag85A, mycolyltransferase, mycolyltransferase, trehalose 6-monomycolate-trehalose, MytC

ECTree

2 Transferases

2.3 Acyltransferases

2.3.1 Transferring groups other than aminoacyl groups

2.3.1.122 trehalose O-mycolyltransferase

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Results	in table
2530	AA Sequence
3	Application
1	CAS Registry Number
8	Cloned(Commentary)
1	Cofactor
5	Crystallization (Commentary)
9	General Information
3	General Stability
20	IC50 Value
40	Inhibitors
4	KM Value [mM]
4	Molecular Weight [Da]
8	Natural Substrates/ Products (Substrates)
27	Organism
2	Pathway
19	PDB ID
7	pH Optimum
1	pH Range
9	Protein Variants
7	Purification (Commentary)
6	Reaction
1	Reaction Type
24	Reference
3	Specific Activity [micromol/min/mg]
26	Substrates and Products (Substrate)
2	Subunits
38	Synonyms
1	Systematic Name
7	Temperature Optimum [°C]
1	Temperature Range [°C]
1	Turnover Number [1/s]

General Information

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General Information on EC 2.3.1.122 - trehalose O-mycolyltransferase

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evolution

Mycobacterium tuberculosis

members of the Ag85 family, Ag85A, Ag85B, and Ag85C, share high sequence and structural homology characterized by an alpha,beta-hydrolase fold and a hydrophobic fibronectin-binding domain. Their active sites are highly conserved, featuring a histidine, aspartic acid or glutamic acid and serine catalytic triad, a hydrophobic tunnel for the lipids and two trehalose binding sites

malfunction

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

704439

physiological function

5 entries