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Information on EC 3.1.1.23 - acylglycerol lipase and Organism(s) Mycobacterium tuberculosis and UniProt Accession O07427
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3.1.1.23 acylglycerol lipaseSpecify your search results
Word Map
- 3.1.1.23
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endocannabinoids
- cannabinoids
- 2-arachidonoylglycerol
- amide
- anandamide
- agonist
- diacylglycerol
- pain
-
arachidonic
- synaptic
- phospholipase
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2-arachidonoyl
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lipolytic
- adipose
- lipases
- prostaglandin
- triacylglycerols
-
anxiety
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activity-based
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presynaptic
-
rimonabant
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nociceptive
-
analgesia
-
antinociceptive
- cannabis
-
cannabimimetic
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neuropathic
- n-arachidonoylethanolamine
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hormone-sensitive
- tetrahydrolipstatin
- 4-nitrophenyl
- n-acylethanolamine
- fluorophosphonate
- diagnostics
- hyperalgesia
- allodynia
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endocannabinoid-mediated
- drug development
- nape-pld
-
depolarization-induced
- medicine
- chlorpyrifos
- synthesis
-
psychoactive
- delta9-tetrahydrocannabinol
-
catalepsy
- pharmacology
- lysophospholipase
- 2-monoacylglycerols
- marijuana
- oleoylethanolamide
-
post-heparin
-
anxiety-like
- palmitoylethanolamide
-
anxiolytic
The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
monoacylglycerol lipase, monoglyceride lipase, mag lipase, rv0183, monoacylglycerol hydrolase, monoglyceride hydrolase, yju3p, mag hydrolase, acylglycerol lipase, msmeg_0220, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
fatty acyl monoester lipase
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monoacylglycerol hydrolase
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monoacylglycerol lipase
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monoglyceridase
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monoglyceride hydrolase
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monoglyceride lipase
monoglyceridyllipase
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monoglyceride lipase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydrolyses glycerol monoesters of long-chain fatty acids
the catalytic triad is composed of Ser110, Asp226 and His256 residues
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carboxylic ester
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SYSTEMATIC NAME
IUBMB Comments
glycerol-ester acylhydrolase
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CAS REGISTRY NUMBER
COMMENTARY
9040-75-9
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-monomyristoyl-rac-glycerol + H2O
myristoate + glycerol
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?
additional information
?
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docking studies with the substrate 1-oleoyl-glycerol in the form of the tetrahedral reaction intermediate. In the best-docking mode, the polar glycerol moiety of the substrate is in direct interaction with catalytically important residues Ser110, His256, Glu257, Met111 and Leu39 from the core region and Tyr181 situated within helix 3 of the cap. No positional preference for sn-1(3) or 2-MGs has been reported for any MGL
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?
additional information
?
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docking studies with the substrate 1-oleoyl-glycerol in the form of the tetrahedral reaction intermediate. In the best-docking mode, the polar glycerol moiety of the substrate is in direct interaction with catalytically important residues Ser110, His256, Glu257, Met111 and Leu39 from the core region and Tyr181 situated within helix 3 of the cap. No positional preference for sn-1(3) or 2-MGs has been reported for any MGL
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?
additional information
?
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Rv0183, as exported enzyme, may be involved in the degradation of the host cell lipids
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?
additional information
?
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substrate specificity, the enzyme hydrolyses monoacylglycerol substrates, both long chain di- and triacylglycerols, although the turnover is lower than with monoacylglycerol, overview, no activity of the recombinant enzyme with lysophospholipid substrates, recombinant Rv0183 hydrolyses synthetic vinyl esters with various acyl chain lengths, chain length dependence, overview
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
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Rv0183, as exported enzyme, may be involved in the degradation of the host cell lipids
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
Mycobacterium tuberculosis MGL cannot be inhibited with JZL-184, a known inhibitor of human MGL. Differences in the binding pocket of mtbMGL compared to human MGL impair JZL-184 inhibition, overview. The human enzyme has an amphipathic cap helix 1 whereas cap helix1 of mtbMGL is mostly hydrophobic. Structure-based analysis for potential inhibitors for mtbMGL. JZL-184 docking study, overview
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additional information
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Mycobacterium tuberculosis MGL cannot be inhibited with JZL-184, a known inhibitor of human MGL. Differences in the binding pocket of mtbMGL compared to human MGL impair JZL-184 inhibition, overview. The human enzyme has an amphipathic cap helix 1 whereas cap helix1 of mtbMGL is mostly hydrophobic. Structure-based analysis for potential inhibitors for mtbMGL. JZL-184 docking study, overview
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additional information
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inactivation by serine esterase inhibitors
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
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50% of maximal activity at pH 6.5, no activity below pH 6.0, maximal activity at pH 7.5-9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
docking studies and structure comparison with the human enzyme, overview. The structure reveals remarkable similarities with MGL from humans (hMGL) in both, the cap region and the alpha/beta core
additional information
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docking studies and structure comparison with the human enzyme, overview. The structure reveals remarkable similarities with MGL from humans (hMGL) in both, the cap region and the alpha/beta core
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
docking studies revealing numerous interactions of mtbMGL to recognize polar and apolar segments of the monoacylglycerol target substrate, and structure comparison with the human enzyme, overview. The three-dimensional structure of mtbMGL reveals an alpha/beta hydrolase fold with an open cap conformation
additional information
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docking studies revealing numerous interactions of mtbMGL to recognize polar and apolar segments of the monoacylglycerol target substrate, and structure comparison with the human enzyme, overview. The three-dimensional structure of mtbMGL reveals an alpha/beta hydrolase fold with an open cap conformation
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme mtbMGL in open conformation, sitting drop vapor diffusion method and microseeding, mixing 500 nl of 10 mg/ml protein solution with 500 nl of crystallization solution containing 0.1 M carboxylic acids, 0.1 M sodium HEPES/MOPS, pH 7.5, 20% ethylene glycol, and 10% PEG 8000, 4 months, 20°C, microseeding by mixing of 400 nl protein solution with 400 nl crystallization solution and 200 nl seeding stock, containing 0.03 M NaNO3, 0.03 M Na2HPO4, 0.03 M (NH4)2SO4, 0.1 M Na HEPES/MOPS, pH 7.8, 12% MPD, 12% PEG 1000 and 12% PEG 3350, 2 weeks, 20°C, X-ray diffraction structure determination and analysis at 1.80 A resolution, molecular replacement using the PDB IDs 3PE6 and 1W53 as search templates
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D226A
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site-directed mutagenesis, active site residue mutation, the catalytic activity is affected
D226N
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site-directed mutagenesis, active site residue mutation, the catalytic activity is affected
H256A
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site-directed mutagenesis, active site residue mutation, the catalytic activity is affected
S110A
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site-directed mutagenesis, active site residue mutation, the catalytic activity is affected
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) CodonPlus by nickel affinity chromatography and gel filtration
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography and gel filtration, removal of the His-tag
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Rv0183, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) CodonPlus
gene Rv0183, DNA and amino acid sequence determination and anaylsis, expression of His-tagged wild-type and mutant enzymes in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
Differences in the binding pocket of mtbMGL compared to human MGL open the possibility for specific inhibition of MGL from the pathogen Mycobacterium tuberculosis and use in the human pathogen treatment
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cotes, K.; Dhouib, R.; Douchet, I.; Chahinian, H.; de Caro, A.; Carriere, F.; Canaan, S.
Characterization of an exported monoglyceride lipase from Mycobacterium tuberculosis possibly involved in the metabolism of host cell membrane lipids
Biochem. J.
408
417-427
2007
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Aschauer, P.; Zimmermann, R.; Breinbauer, R.; Pavkov-Keller, T.; Oberer, M.
The crystal structure of monoacylglycerol lipase from M. tuberculosis reveals the basis for specific inhibition
Sci. Rep.
8
8948
2018
Mycobacterium tuberculosis (O07427), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (O07427), Mycobacterium tuberculosis ATCC 25618 (O07427)
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Release 2023.1 (January 2023)
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