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Information on EC 3.1.1.23 - acylglycerol lipase and Organism(s) Bacillus subtilis and UniProt Accession Q79F14

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.23 acylglycerol lipase
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This record set is specific for:
Bacillus subtilis
UNIPROT: Q79F14 not found.
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Word Map
The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
monoacylglycerol lipase, monoglyceride lipase, mag lipase, rv0183, monoacylglycerol hydrolase, monoglyceride hydrolase, yju3p, mag hydrolase, acylglycerol lipase, msmeg_0220, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
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
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monoglyceridyllipase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
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PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
glycerol-ester acylhydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
9040-75-9
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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
4-nitrophenyl caprate + H2O
4-nitrophenol + capric acid
show the reaction diagram
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-
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
show the reaction diagram
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-
?
4-nitrophenyl-caproate + H2O
4-nitrophenol + caproic acid
show the reaction diagram
-
-
?
4-nitrophenyl-laurate + H2O
4-nitrophenol + lauric acid
show the reaction diagram
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-
?
4-nitrophenyl-myristate + H2O
4-nitrophenol + myristic acid
show the reaction diagram
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-
?
4-nitrophenyl-palmitate + H2O
4-nitrophenol + palmitic acid
show the reaction diagram
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-
?
4-nitrophenyl-stearate + H2O
4-nitrophenol + stearic acid
show the reaction diagram
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?
additional information
?
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
19490
calculated from amino acid sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, benzamidine is essential for crystallization
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A76G
reduced thermostability, increased stability at pH 5-7, substitution converts the esterase into a monoacylglycerol hydrolase
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
wild-type enzyme is stable, A76G mutant loses 50% activity after 8 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yoneda, K.; Nishimura, T.; Katunuma, N.; Imamura, S.; Nitta, K.; Tsuge, H.
Crystallization and preliminary X-ray crystallographic studies of monoacylglycerol lipase of the moderately thermophilic Bacillus sp. H-257
Acta Crystallogr. Sect. D
58
1232-1233
2002
Bacillus subtilis, Bacillus subtilis H-257
Manually annotated by BRENDA team
Eggert, T.; Pencreac'h, G.; Douchet, I.; Verger, R.; Jaeger, K.E.
A novel extracellular esterase from Bacillus subtilis and its conversion to a monoacylglycerol hydrolase
Eur. J. Biochem.
267
6459-6469
2000
Bacillus subtilis (Q79F14), Bacillus subtilis
Manually annotated by BRENDA team