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Information on EC 2.3.1.122 - trehalose O-mycolyltransferase
for references in articles please use BRENDA:EC2.3.1.122
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.1 Transferring groups other than aminoacyl groups
2.3.1.122 trehalose O-mycolyltransferase
IUBMB Comments
Catalyses the exchange of mycolic acid between trehalose, trehalose mycolate and trehalose bismycolate. Trehalose 6-palmitate can also act as donor.
The expected taxonomic range for this enzyme is: Bacteria, Archaea
- 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 Schemes
showSynonyms
ag85a, antigen 85a, ag85c, mycolyltransferase, antigen 85c, mycolyl-transferase ag85a, mycoloyl transferase, cg0413, fbpa mycolyltransferase, alpha,alpha'-trehalose 6-monomycolate:alpha,alpha'-trehalose mycolyltransferase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ag85C
alpha,alpha'-trehalose 6-monomycolate:alpha,alpha'-trehalose mycolyltransferase
-
-
-
-
antigen 85A
antigen 85C
cg0413
CMT1
corynomycoloyl transferase C
FbpA mycolyltransferase
mycoloyl transferase
mycolyltransferase
mycolyltransferase, trehalose 6-monomycolate-trehalose
-
-
-
-
MytC
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 alpha,alpha-trehalose 6-mycolate = alpha,alpha-trehalose + alpha,alpha-trehalose 6,6'-bismycolate
2 alpha,alpha-trehalose 6-mycolate = alpha,alpha-trehalose + alpha,alpha-trehalose 6,6'-bismycolate
reaction catalyzed by antigen 85B complex involved in cell wall biosynthesis. Previously unsuspected role of 85B protein in pathogenesis of tuberculosis
-
2 alpha,alpha-trehalose 6-mycolate = alpha,alpha-trehalose + alpha,alpha-trehalose 6,6'-bismycolate
reaction catalyzed by 3 members of the Ag85 complex in vitro, namely FbpA, FbpB and FbpC2
-
2 alpha,alpha-trehalose 6-mycolate = alpha,alpha-trehalose + alpha,alpha-trehalose 6,6'-bismycolate
reaction mechanism via enzyme complexed with the tetrahedral transition state and mycolic acid covalently attached to the enzyme, the catalytic triad is formed by Ser124, Glu228 and His260
-
2 alpha,alpha-trehalose 6-mycolate = alpha,alpha-trehalose + alpha,alpha-trehalose 6,6'-bismycolate
reaction mechanism via enzyme complexed with the tetrahedral transition state and mycolic acid covalently attached to the enzyme, the catalytic triad is formed by Ser124, Glu228 and His260
2 alpha,alpha-trehalose 6-mycolate = alpha,alpha-trehalose + alpha,alpha-trehalose 6,6'-bismycolate
reaction mechanism via enzyme complexed with the tetrahedral transition state and mycolic acid covalently attached to the enzyme, the catalytic triad is formed by Ser124, Glu228 and His260
-
-
2 alpha,alpha-trehalose 6-mycolate = alpha,alpha-trehalose + alpha,alpha-trehalose 6,6'-bismycolate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
mycolate biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
alpha,alpha-trehalose-6-mycolate:alpha,alpha-trehalose-6-mycolate 6'-mycolyltransferase
Catalyses the exchange of mycolic acid between trehalose, trehalose mycolate and trehalose bismycolate. Trehalose 6-palmitate can also act as donor.
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CAS REGISTRY NUMBER
COMMENTARY
111694-11-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 alpha,alpha-trehalose 6-monomycolate
alpha,alpha-trehalose 6,6'-dimycolate + alpha,alpha-trehalose
2 alpha,alpha-trehalose 6-mycolate
alpha,alpha-trehalose + alpha,alpha-trehalose 6,6'-bismycolate
alpha,alpha'-trehalose 6-monomycolate + alpha,alpha'-trehalose 6-monomycolate
alpha,alpha'-trehalose 6,6'-dimycolate + alpha,alpha'-trehalose
-
Substrates: -
Products: -
Products: -
?
alpha,alpha-trehalose 6,6'-dimycolate + PorA
alpha,alpha-trehalose 6-monomycolate + mycoloyl-PorA
alpha,alpha-trehalose 6,6'-dimycolate + PorH
alpha,alpha-trehalose 6-monomycolate + mycoloyl-PorH
alpha,alpha-trehalose 6-mycolate
alpha,alpha-trehalose + alpha,alpha-trehalose 6,6'-bismycolate
alpha,alpha-trehalose 6-mycolate + alpha,alpha-trehalose
alpha,alpha-trehalose + alpha,alpha-trehalose 6-mycolate
-
Substrates: -
Products: -
Products: -
r
alpha,alpha-trehalose 6-palmitate + trehalose
alpha,alpha-trehalose + alpha,alpha-trehalose 6-palmitate
-
Substrates: -
Products: -
Products: -
r
alpha,alpha-trehalose monomycolate + D-glucose
D-glucose monomycolate + alpha,alpha-trehalose
2 alpha,alpha-trehalose 6-monomycolate
alpha,alpha-trehalose 6,6'-dimycolate + alpha,alpha-trehalose
-
Substrates: -
Products: -
Products: -
?
2 alpha,alpha-trehalose 6-monomycolate
alpha,alpha-trehalose 6,6'-dimycolate + alpha,alpha-trehalose
Substrates: 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
Products: -
Products: -
?
2 alpha,alpha-trehalose 6-monomycolate
alpha,alpha-trehalose 6,6'-dimycolate + alpha,alpha-trehalose
-
Substrates: 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
Products: -
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?
2 alpha,alpha-trehalose 6-mycolate
alpha,alpha-trehalose + alpha,alpha-trehalose 6,6'-bismycolate
-
Substrates: -
Products: -
Products: -
?
2 alpha,alpha-trehalose 6-mycolate
alpha,alpha-trehalose + alpha,alpha-trehalose 6,6'-bismycolate
-
Substrates: -
Products: -
Products: -
r
alpha,alpha-trehalose 6,6'-dimycolate + PorA
alpha,alpha-trehalose 6-monomycolate + mycoloyl-PorA
Substrates: O-acylation of pore-forming protein
Products: -
Products: -
?
alpha,alpha-trehalose 6,6'-dimycolate + PorA
alpha,alpha-trehalose 6-monomycolate + mycoloyl-PorA
Substrates: O-acylation of pore-forming protein
Products: -
Products: -
?
alpha,alpha-trehalose 6,6'-dimycolate + PorH
alpha,alpha-trehalose 6-monomycolate + mycoloyl-PorH
Substrates: O-acylation of pore-forming protein
Products: -
Products: -
?
alpha,alpha-trehalose 6,6'-dimycolate + PorH
alpha,alpha-trehalose 6-monomycolate + mycoloyl-PorH
Substrates: O-acylation of pore-forming protein
Products: -
Products: -
?
alpha,alpha-trehalose 6-mycolate
alpha,alpha-trehalose + alpha,alpha-trehalose 6,6'-bismycolate
-
Substrates: -
Products: -
Products: -
?
alpha,alpha-trehalose 6-mycolate
alpha,alpha-trehalose + alpha,alpha-trehalose 6,6'-bismycolate
Substrates: -
Products: -
Products: -
?
alpha,alpha-trehalose 6-mycolate
alpha,alpha-trehalose + alpha,alpha-trehalose 6,6'-bismycolate
Substrates: -
Products: -
Products: -
?
alpha,alpha-trehalose monomycolate + D-glucose
D-glucose monomycolate + alpha,alpha-trehalose
-
Substrates: Mycobacterium tuberculosis and Mycobacterium avium, replace TDM with glucose monomycolate by borrowing host-derived glucose as an alternative substrate for the FbpA mycolyltransferase
Products: -
Products: -
?
alpha,alpha-trehalose monomycolate + D-glucose
D-glucose monomycolate + alpha,alpha-trehalose
Substrates: 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
Products: -
Products: -
?
alpha,alpha-trehalose monomycolate + D-glucose
D-glucose monomycolate + alpha,alpha-trehalose
-
Substrates: D-glucose is used as an alternative acceptor substrate. FbpA mycolyltransferase from Mycobacterium leprae shows only trace of glucose monomycolate is detected
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme additionally catalyzes the transfer of the fatty acid residue to yield O-acylated polypeptides
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme additionally catalyzes the transfer of the fatty acid residue to yield O-acylated polypeptides
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme additionally catalyzes the transfer of the fatty acid residue to yield O-acylated polypeptides
Products: -
Products: -
?
additional information
?
-
-
Substrates: evaluation of the substrate tolerance of Ag85 isoforms, development of a broad Ag85 substrate, overview. Modifications on every position of the sugar scaffold are tolerated, including even C-1 methyl groups at the crowded anomeric linkages, positive charges, such as in the 2-amino-trehalose and even stereochemically incorrect 2,2'-di-fluoro-alpha,beta-mannotrehalose. Even a previously reported inhibitor 6-azido-trehalose, and putative tetrahedral intermediate analogs, such as trehalose-6-phosphate, are also processed. 2,2'-dideoxy-lyxo-trehalose is no substrate
Products: -
Products: -
?
additional information
?
-
Substrates: the binding of the incoming acceptor molecule drives the protein to form an active conformation, the second half-reaction could therefore proceed through a direct or indirect activation pathway upon acceptor molecule binding. The beta-hydroxy group of mycolic acid plays a direct role in the second half-reaction of Ag85 catalysis
Products: -
Products: -
-
additional information
?
-
Substrates: the binding of the incoming acceptor molecule drives the protein to form an active conformation, the second half-reaction could therefore proceed through a direct or indirect activation pathway upon acceptor molecule binding. The beta-hydroxy group of mycolic acid plays a direct role in the second half-reaction of Ag85 catalysis
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme, in form of DNA and protein or peptide fragments, is immunogenic in C57BL/6 mice and effective as tuberculosis vaccine against Mycobacterium tuberculosis strain H37Rv, alone and especially in combination with PstS3 DNA and/or protein, detailed overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: exchange of mycolyl group, highly specific for alpha,alpha'-trehalose as the mycolate acceptor, less specific for the acyl donor group
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 alpha,alpha-trehalose 6-mycolate
alpha,alpha-trehalose + alpha,alpha-trehalose 6,6'-bismycolate
alpha,alpha-trehalose 6-mycolate
alpha,alpha-trehalose + alpha,alpha-trehalose 6,6'-bismycolate
alpha,alpha-trehalose 6-mycolate + alpha,alpha-trehalose
alpha,alpha-trehalose + alpha,alpha-trehalose 6-mycolate
-
Substrates: -
Products: -
Products: -
r
additional information
?
-
-
Substrates: the enzyme, in form of DNA and protein or peptide fragments, is immunogenic in C57BL/6 mice and effective as tuberculosis vaccine against Mycobacterium tuberculosis strain H37Rv, alone and especially in combination with PstS3 DNA and/or protein, detailed overview
Products: -
Products: -
?
2 alpha,alpha-trehalose 6-mycolate
alpha,alpha-trehalose + alpha,alpha-trehalose 6,6'-bismycolate
-
Substrates: -
Products: -
Products: -
?
2 alpha,alpha-trehalose 6-mycolate
alpha,alpha-trehalose + alpha,alpha-trehalose 6,6'-bismycolate
-
Substrates: -
Products: -
Products: -
r
alpha,alpha-trehalose 6-mycolate
alpha,alpha-trehalose + alpha,alpha-trehalose 6,6'-bismycolate
-
Substrates: -
Products: -
Products: -
?
alpha,alpha-trehalose 6-mycolate
alpha,alpha-trehalose + alpha,alpha-trehalose 6,6'-bismycolate
Substrates: -
Products: -
Products: -
?
alpha,alpha-trehalose 6-mycolate
alpha,alpha-trehalose + alpha,alpha-trehalose 6,6'-bismycolate
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no requirement of cofactors such as ATP or CoA
-
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-methyl ethyl butylphosphonate
-
IC50: 0.010 mM
(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-methyl ethyl tetradecylphosphonate
-
IC50: 0.0410 mM
(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)methyl ethyl heptylphosphonate
-
IC50: 0.0013 mM
(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)methyl ethyl nonylphosphonate
-
IC50: 0.0871 mM
(2S)-N-hydroxy-1-[4-(1,1'-biphenyl)-3,6-dihydropyridine-1(2H)-sulfonyl]piperidine-2-carboxamide
compound identified by virtual screening, shows considerable hydrogen bonds with Ag85C during 100 ns simulation and predicted to be non-hepatotoxic, non-carcinogen, non-mutagenic and non-cytotoxic
1-[(2S)-2-benzyl-2-(hydroxymethyl)morpholin-4-yl]-2-pyrimidin-2-yloxyethanone
compound identified by virtual screening, shows considerable hydrogen bonds with Ag85C during 100 ns simulation and predicted to be non-hepatotoxic, non-carcinogen, non-mutagenic and non-cytotoxic
2-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-ethyl ethyl butylphosphonate
-
IC50: 0.0507 mM
2-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-ethyl ethyl nonylphosphonate
-
IC50: 0.0257 mM
2-amino-6-propyl-4,5,6,7-tetrahydro-1-benzothiophene-3-carbonitrile
i.e. I3-AG85, enzyme inhibition leads to accumulation of trehalose monomycolate and disruption of the bacterial envelope, I3-AG85 also inhibits Mycobacterium tuberculosis survival in infected primary macrophages. Binding of I3-AG85 to Ag85C is similar to its binding to the artificial substrate octylthioglucoside, overview
2-[[[(3R*,4R*)-4-(hydroxymethyl)-1-(2-methoxy-3-methylbenzoyl)pyrrolidin-3-yl]methyl](methyl)amino]ethanol
compound identified by virtual screening, shows considerable hydrogen bonds with Ag85C during 100 ns simulation and predicted to be non-hepatotoxic, non-carcinogen, non-mutagenic and non-cytotoxic
6-azido-6-deoxytrehalose
-
inhibits all three members of Ag85 complex in vitro
ethyl hydrogen 4-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)butylphosphonate
-
IC50: 0.110 mM
tetrahydrolipstatin
covalent inhibition. The enzyme undergoes structural changes upon acylation, and positioning of the peptidyl arm of tetrahydrolipstain limits hydrolysis of the acyl-enzyme adduct
Tween 80
-
strong, might disrupt necessary structure of the TM vesicle/micelle
[(1R,2S,4S,5S,7R,9S,10S)-12-(hydroxymethyl)-4,5,15-trimethoxy-4,5-dimethyl-3,6,17-trioxatetracyclo[8.7.0.02,7.011,16]heptadeca-11,13,15-trien-9-yl]methanol
compound identified by virtual screening, shows considerable hydrogen bonds with Ag85C during 100 ns simulation and predicted to be non-hepatotoxic, non-carcinogen, non-mutagenic and non-cytotoxic
additional information
-
design of mechanism-based inhibitors, growth inhibition assay, molecular docking, overview
-
additional information
design of mechanism-based inhibitors, growth inhibition assay, molecular docking, 2-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)ethyl 1-butanesulfonate and 2-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)ethyl 1-octanesulfonate show no enzyme inhibition but are selectively cytotoxic against the breast cancer cell line MDA-MB231, overview
-
additional information
-
inhibitor screening by molecular docking, overview
-
additional information
-
design and synthesis of a trehalose analogue library for identification of Ag85 inhibitors, modifications of the trehalose scaffold, overview
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.043
alpha,alpha-trehalose 6-monomycolate
-
mutant L130S, short-chain trehalose monomycolate is used as a substrate, Vmax: 4.27 nmol/min/nmol
0.459
alpha,alpha-trehalose 6-monomycolate
-
wild-type, short-chain trehalose monomycolate is used as a substrate, Vmax: 3.83 nmol/min/nmol
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-methyl ethyl butylphosphonate
Mycobacterium avium
-
IC50: 0.010 mM
0.041
(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-methyl ethyl tetradecylphosphonate
Mycobacterium avium
-
IC50: 0.0410 mM
0.0013
(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)methyl ethyl heptylphosphonate
Mycobacterium avium
-
IC50: 0.0013 mM
0.0871
(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)methyl ethyl nonylphosphonate
Mycobacterium avium
-
IC50: 0.0871 mM
0.0043
1-(3-phenoxy)benzyl 1-octanesulfonate
Mycobacterium tuberculosis
IC50: 0.0043 mM
0.0507
2-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-ethyl ethyl butylphosphonate
Mycobacterium avium
-
IC50: 0.0507 mM
0.0257
2-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-ethyl ethyl nonylphosphonate
Mycobacterium avium
-
IC50: 0.0257 mM
0.11
ethyl hydrogen 4-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)butylphosphonate
Mycobacterium avium
-
IC50: 0.110 mM
0.002
ethyl 3-phenoxybenzyl butylphosphonate
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
compared to FbpA of Mycobacterium leprae activity of FbpA is strikingly enhanced in Mycobacterium avium
additional information
-
compared to FbpA of Mycobacterium tuberculosis and Mycobacterium avium activity of FbpA is reduced in Mycobacterium leprae
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9
-
45% of maximal activity at pH 5.0, 30% of maximal activity at pH 9.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
and clinical isolates MT103 and MYC1554, dru-resistant Ag85C mutants
Uniprot
brenda
and clinical isolates MT103 and MYC1554, dru-resistant Ag85C mutants
Uniprot
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
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
physiological function
malfunction
inhibition of Ag85 protein family enzymes through substrate analogs hinders growth of mycobacteria and inhibition of Ag85C leads to accumulation of trehalose monomycolate
malfunction
-
inhibition of Ag85 protein family enzymes through substrate analogs hinders growth of mycobacteria and inhibition of Ag85C leads to accumulation of trehalose monomycolate
-
physiological function
-
the enzyme is responsible for converting trehalose monomycolate to trehalose dimycolate, which contributes to cell wall stability
physiological function
the mycoloyl transferase activity of antigen 85 (Ag85) protein family, consisting of Ag85A, -B, and -C, generates trehalose dimycolate, an envelope lipid essential for Mycobacterium tuberculosis virulence, and cell wall arabinogalactan-linked mycolic acids
physiological function
inactivation of corynomycoloyl transferase C specifically abolishes the O-modification of the pore-forming proteins PorA and PorH, which is critical for their biological activity
physiological function
-
the mycoloyl transferase activity of antigen 85 (Ag85) protein family, consisting of Ag85A, -B, and -C, generates trehalose dimycolate, an envelope lipid essential for Mycobacterium tuberculosis virulence, and cell wall arabinogalactan-linked mycolic acids
-
physiological function
-
inactivation of corynomycoloyl transferase C specifically abolishes the O-modification of the pore-forming proteins PorA and PorH, which is critical for their biological activity
-
Show AA Sequence and Transmembrane Helices (2530 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30000
-
FbpA: SDS-PAGE, Western Blot, aminoacid sequence. FbpB: aminoacid sequence. FbpC2: SDS-PAGE, Western Blot, aminoacid sequence
33000
SDS-PAGE, detection of a fusion protein consiting of a His-tag and the mature Ag85A protein
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
three-dimensional model based on crystal structure of related enzymes, comparison of enzymes
-
native protein, to 1.75 A resolution. Strucutre shows the presence of a unique loop that is absent from enzym