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Information on EC 2.3.1.122 - trehalose O-mycolyltransferase and Organism(s) Mycobacterium tuberculosis and UniProt Accession P9WQN8

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IUBMB Comments
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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Mycobacterium tuberculosis
UNIPROT: P9WQN8
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The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ag85C
cf. EC 2.3.1.20
ag85C
alpha,alpha'-trehalose 6-monomycolate:alpha,alpha'-trehalose mycolyltransferase
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-
-
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antigen 85C
mycoloyl transferase
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mycolyltransferase
mycolyltransferase, trehalose 6-monomycolate-trehalose
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-
-
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 alpha,alpha-trehalose 6-mycolate = alpha,alpha-trehalose + alpha,alpha-trehalose 6,6'-bismycolate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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-
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PATHWAY SOURCE
PATHWAYS
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
111694-11-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 alpha,alpha-trehalose 6-mycolate
alpha,alpha-trehalose + alpha,alpha-trehalose 6,6'-bismycolate
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose 6-mycolate
alpha,alpha-trehalose + alpha,alpha-trehalose 6,6'-bismycolate
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 alpha,alpha-trehalose 6-mycolate
alpha,alpha-trehalose + alpha,alpha-trehalose 6,6'-bismycolate
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose 6-mycolate
alpha,alpha-trehalose + alpha,alpha-trehalose 6,6'-bismycolate
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
(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-(3-phenoxy)benzyl 1-octanesulfonate
IC50: 0.0043 mM
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-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
3-Phenoxybenzyl alcohol
trehalose mimetic inhibitor
6-azido-6-deoxytrehalose
-
inhibits all three members of Ag85 complex in vitro
ethyl 3-phenoxybenzyl butylphosphonate
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-
N-(hydroxyethyl)phthalimide
trehalose mimetic inhibitor
[(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
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0043
1-(3-phenoxy)benzyl 1-octanesulfonate
Mycobacterium tuberculosis
IC50: 0.0043 mM
0.002
ethyl 3-phenoxybenzyl butylphosphonate
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cf. EC 2.3.1.20
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
-
FbpA: SDS-PAGE, Western Blot, aminoacid sequence. FbpB: aminoacid sequence. FbpC2: SDS-PAGE, Western Blot, aminoacid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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FbpA: 1 * 30000, SDS-PAGE. FbpC2: 1 * 30000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of Ag85C covalently modified by esterase inhibitor tetrahydrolipstatin
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S148A
mutant lacks observable transesterase activity but exhibits hydrolase activity at a lower level than that of wild-type
S148T
mutant lacks observable transesterase activity but exhibits hydrolase activity at a lower level than that of wild-type
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant proteins purified by affinity chromatography on Ni2+ charged His-trap columns
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of FbpA, FbpB and FbpC2 in Escherichia coli, FbpB poorly expressed due to differential efficiency of mRNA translation
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recombinant expression as C-terminally His-tagged enzyme
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
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antigen 85 proteins are potential drug targets
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wilkinson, R.J.; DesJardin, L.E.; Islam, N.; Gibson, B.M.; Kanost, R.A.; Wilkinson, K.A.; Poelman, D.; EisenachK.D.; Toossi, Z.
An increase in expression of a tuberculosis mycolyl transferase gene (fbpB) gene occurs early after infection of human monocytes
Mol. Microbiol.
39
813-821
2001
Mycobacterium tuberculosis
Manually annotated by BRENDA team
Kreme, L.; Maughan, W.N.; Wilson, R.A.; Dover, L.G.; Besra, G.S.
The M. tuberculosis antigen 85 complex and mycolyltransferase activity
Lett. Appl. Microbiol.
34
233-237
2002
Mycobacterium tuberculosis
Manually annotated by BRENDA team
Kovac, A.; Wilson, R.A.; Besra, G.S.; Filipic, M.; Kikelj, D.; Gobec, S.
New lipophilic phthalimido- and 3-phenoxybenzyl sulfonates: inhibition of antigen 85C mycolyltransferase activity and cytotoxicity
J. Enzyme Inhib. Med. Chem.
21
391-397
2006
Mycobacterium tuberculosis (P9WQN9), Mycobacterium tuberculosis H37Rv (P9WQN9)
Manually annotated by BRENDA team
Warrier, T.; Tropis, M.; Werngren, J.; Diehl, A.; Gengenbacher, M.; Schlegel, B.; Schade, M.; Oschkinat, H.; Daffe, M.; Hoffner, S.; Eddine, A.N.; Kaufmann, S.H.
Antigen 85C inhibition restricts Mycobacterium tuberculosis growth through disruption of cord factor biosynthesis
Antimicrob. Agents Chemother.
56
1735-1743
2012
Mycobacterium tuberculosis (P9WQN9), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WQN9)
Manually annotated by BRENDA team
Gahoi, S.; Mandal, R.S.; Ivanisenko, N.; Shrivastava, P.; Jain, S.; Singh, A.K.; Raghunandanan, M.V.; Kanchan, S.; Taneja, B.; Mandal, C.; Ivanisenko, V.A.; Kumar, A.; Kumar, R.; Open Source Drug Discovery Consortium; Ramachandran, S.
Computational screening for new inhibitors of M. tuberculosis mycolyltransferases antigen 85 group of proteins as potential drug targets
J. Biomol. Struct. Dyn.
1
30-43
2012
Mycobacterium tuberculosis
Manually annotated by BRENDA team
Backus, K.M.; Boshoff, H.I.; Barry, C.S.; Boutureira, O.; Patel, M.K.; DHooge, F.; Lee, S.S.; Via, L.E.; Tahlan, K.; Barry, C.E.; Davis, B.G.
Uptake of unnatural trehalose analogs as a reporter for Mycobacterium tuberculosis
Nat. Chem. Biol.
7
228-235
2011
Mycobacterium tuberculosis
Manually annotated by BRENDA team
Goins, C.M.; Dajnowicz, S.; Smith, M.D.; Parks, J.M.; Ronning, D.R.
Mycolyltransferase from Mycobacterium tuberculosis in covalent complex with tetrahydrolipstatin provides insights into antigen 85 catalysis
J. Biol. Chem.
293
3651-3662
2018
Mycobacterium tuberculosis (P9WQN8), Mycobacterium tuberculosis CDC 1551 (P9WQN8)
Manually annotated by BRENDA team
Pant, R.; Joshi, A.; Maiti, P.; Nand, M.; Pande, V.; Chandra, S.
Identification of potential mycolyltransferase Ag85C inhibitors of Mycobacterium tuberculosis H37Rv via virtual high throughput screening and binding free energy studies
J. Mol. Graph. Model.
98
107584
2020
Mycobacterium tuberculosis (P9WQP3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WQP3), Mycobacterium tuberculosis H37Rv
Manually annotated by BRENDA team