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Information on EC 3.1.1.56 - methylumbelliferyl-acetate deacetylase and Organism(s) Homo sapiens

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.56 methylumbelliferyl-acetate deacetylase
IUBMB Comments
Acts on short-chain acyl esters of 4-methylumbelliferone, but not on naphthyl, indoxyl or thiocholine esters.
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This record set is specific for:
Homo sapiens
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
ested, serine thioesterase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
EsteD
-
-
esterase D
S-formylglutathione hydrolase
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
4-methylumbelliferyl-acetate acylhydrolase
Acts on short-chain acyl esters of 4-methylumbelliferone, but not on naphthyl, indoxyl or thiocholine esters.
CAS REGISTRY NUMBER
COMMENTARY hide
83380-83-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-naphthyl acetate + H2O
1-naphthol + acetate
show the reaction diagram
-
-
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferone + acetate
show the reaction diagram
4-methylumbelliferyl butyrate + H2O
4-methylumbelliferone + butyrate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
-
-
-
-
?
naphthyl acetate + H2O
naphthol + acetate
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
acts on short chain acyl esters of 4-methylumbelliferone, but not on naphthyl, indoxyl or thiocholine esters
-
-
?
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
4-methylumbelliferyl acetate + H2O
4-methylumbelliferone + acetate
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Dansylglutamylglycylarginyl chloromethyl ketone
-
weak
diisopropyl fluorophosphate
-
-
iodoacetamide
-
weak
phenylmethylsulfonyl fluoride
additional information
-
relatively insensitive to: 4-nitrophenyl phosphate and acetozolamide
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.5 - 3.1
1-naphthyl acetate
2.9 - 4
2-naphthyl acetate
0.067
4-Methylumbelliferyl butyrate
-
pH 5.2, 37°C, isoenzymes Es D1 and Es D2
0.9
4-nitrophenyl acetate
-
pH 5.2, 37°C, isoenzymes Es D1 and Es D2
0.55 - 0.83
4-nitrophenyl butyrate
0.01 - 0.03
4-yethylumbelliferyl acetate
1.7
Naphthyl acetate
-
pH 6.0, 23°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 5.5
-
methylumbelliferyl acetate, methylumbelliferyl butyrate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9.5
-
pH 5: about 40% of activity maximum, pH 9.5: about 30% of activity maximum
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.7
-
theoretical
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
autoantibodies detectable in patients with Behcet’s disease (BD, 25%), Vogt-Koyanagi-Harada disease (VKH, 25%), and sarcoidosis (17.6%)
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
additional information
-
proteomic analysis of bone marrow and peripheral blood mononuclear cells in acute myeloid leukemia patients and healthy subjects
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ESTD_HUMAN
282
0
31463
Swiss-Prot
other Location (Reliability: 3)
EST1_HUMAN
567
0
62521
Swiss-Prot
Secretory Pathway (Reliability: 2)
EST2_HUMAN
559
0
61807
Swiss-Prot
Mitochondrion (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27000
-
isoenzyme Es D1 and Es D2, gel filtration
31800
-
theoretical
34000
-
1 * 34000, isoenzyme Es D1 and Es D2, SDS-PAGE
35000
-
2 * 35000, isoenzyme Es D1 and Es D2, SDS-PAGE with or without 2-mercaptoethanol
76000
-
isoenzyme Es D1 and Es D2, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
monomer
-
1 * 34000, isoenzyme Es D1 and Es D2, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
isoenzymes contain very little if any carbohydrate
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop: 16°C, 3 days, reservoir solution: sodium citrate pH 5.6, 200 mM ammonium acetate, 30% (w/v) polyethylene glycol (PEG) 4000, crystal: space group P2(1), unit cell parameters: a: 51.54, b: 70.72, c: 65.01, alpha: 90°, beta: 108.84°, gamma: 90°, 2 molecules in the asymmetric unit, molecular replacement using PDB: 1PV1, co-crystallization and soaking with substrate failed, structure: several insertions in canonical alpha/beta-hydrolase fold, GxSxG motif, active site in positively charged cleft including residues S149, D226, and H260, and aromatic residues (H148, F172 W183, F228, H260, Y262) lined at the surface, catalysis mediated by residues S153, H264, and D230, oxyanion hole formed by e.g. L54 and M150
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D226A
-
4.3% of wild-type activity
D226N
-
9% of wild-type activity
H260A
-
3% of wild-type activity
H260Q
-
1.3% of wild-type activity
L54A
-
83% of wild-type activity
M150
-
162% of wild-type activity, possibly due to reduced steric hindrance
S149A
-
catalytically inactive
S149T
-
1.3% of wild-type activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
15 min, about 25% loss of activity
50
-
15 min, about 40% loss of activity
70
-
15 min, about 75% loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by nickel-affinity chromatography (elution: 300 mM imidazole) followed by cleavage of His-tag by tobacco etch virus (TEV) protease, a second nickel-affinity chromatography, and size-exclusion chromatography (Superdex G75) in presence of 1 mM dithiothreitol
-
isoenzyme Es D1 and Es D2
-
partial, esterase D is identical to sialic acid-specific O-acetylesterase
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
from brain cDNA in pMCSG7 for inducible expression with N-terminal hexa-His-tag in Escherichia coli BL21(DE3)
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
medicine
-
enzyme should serve as a genetic marker of retinoblstome
molecular biology
-
studying the physiological role
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Okada, Y.; Wakabayashi, K.
Purification and characterization of esterases D-1 and D-2 from human erythrocytes
Arch. Biochem. Biophys.
263
130-136
1988
Homo sapiens
Manually annotated by BRENDA team
Hopkinson, D.A.; Mestriner, M.A.; Cortner, J.; Harris, H.
Esterase D: a new human polymorphism
Ann. Hum. Genet.
37
119-137
1973
Homo sapiens
Manually annotated by BRENDA team
Weidinger, S.; Henke, J.
Two new esterase D (ESD) variants revealed by isoelectric focusing in agarose gel
Electrophoresis
9
429-432
1988
Homo sapiens
Manually annotated by BRENDA team
Alonso, A.; Visedo, G.; Sancho, M.; Fernandez-Piqueras, J.
Identification of human esterase D subunits from the homodimeric and heterodimeric forms of five phenotypes by a new two-dimensional isoelectric focusing method
Electrophoresis
12
348-351
1991
Homo sapiens
Manually annotated by BRENDA team
Matsuo, K.; Kobayashi, K.; Hagiwara, K.; Kajii, T.
Purification and characterization of esterases D1 and D2 from human erythrocytes. Evidence that they are monomers
Eur. J. Biochem.
153
217-222
1985
Homo sapiens
Manually annotated by BRENDA team
Varki, A.; Muchmore, E.; Diaz, S.
A sialic acid-specific O-acetylesterase in human erythrocytes: possible identity with esterase D, the genetic marker of retinoblastomas and Wilson disease
Proc. Natl. Acad. Sci. USA
83
882-886
1986
Homo sapiens
Manually annotated by BRENDA team
Lee, W.H.; Wheatley, W.; Benedict, W.F.; Huang, C.M.
Purification, biochemical characterization, and biological function of human esterase D
Proc. Natl. Acad. Sci. USA
83
6790-6794
1986
Homo sapiens
Manually annotated by BRENDA team
Lee, E.Y.H.; Lee, W.H.
Molecular cloning of the human esterase D gene, a genetic marker of retinoblastoma
Proc. Natl. Acad. Sci. USA
83
6337-6341
1986
Homo sapiens
Manually annotated by BRENDA team
Wu, D.; Li, Y.; Song, G.; Zhang, D.; Shaw, N.; Liu, Z.J.
Crystal structure of human esterase D: a potential genetic marker of retinoblastoma
FASEB J.
23
1441-1446
2009
Homo sapiens
Manually annotated by BRENDA team
Okunuki, Y.; Usui, Y.; Kezuka, T.; Hattori, T.; Masuko, K.; Nakamura, H.; Yudoh, K.; Goto, H.; Usui, M.; Nishioka, K.; Kato, T.; Takeuchi, M.
Proteomic surveillance of retinal autoantigens in endogenous uveitis: implication of esterase D and brain-type creatine kinase as novel autoantigens
Mol. Vis.
14
1094-1104
2008
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Kazmierczak, M.; Luczak, M.; Lewandowski, K.; Handschuh, L.; Czyz, A.; Jarmuz, M.; Gniot, M.; Michalak, M.; Figlerowicz, M.; Komarnicki, M.
Esterase D and gamma 1 actin level might predict results of induction therapy in patients with acute myeloid leukemia without and with maturation
Med. Oncol.
30
725
2013
Homo sapiens
Manually annotated by BRENDA team