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PDBsum entry 1tqh
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Contents |
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* Residue conservation analysis
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Enzyme class:
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E.C.3.1.1.1
- carboxylesterase.
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Reaction:
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a carboxylic ester + H2O = an alcohol + a carboxylate + H+
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carboxylic ester
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+
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H2O
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=
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alcohol
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+
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carboxylate
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+
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H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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J Mol Biol
342:551-561
(2004)
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PubMed id:
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Covalent reaction intermediate revealed in crystal structure of the Geobacillus stearothermophilus carboxylesterase Est30.
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P.Liu,
Y.F.Wang,
H.E.Ewis,
A.T.Abdelal,
C.D.Lu,
R.W.Harrison,
I.T.Weber.
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ABSTRACT
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Est30 is a thermophilic carboxylesterase cloned from Geobacillus
stearothermophilus that showed optimal hydrolysis of esters with short acyl
chains at 70 degrees C. Est30 is a member of a new family of carboxylesterases
with representatives in other Gram-positive bacteria. The crystal structure has
been determined at 1.63A resolution using multiple anomalous dispersion data.
The two-domain crystal structure showed a large domain with a modified
alpha/beta hydrolase core including a seven, rather than an eight-stranded beta
sheet, and a smaller cap domain comprising three alpha helices. The catalytic
triad consists of residues Ser94, Asp193, and His223. A 100Da tetrahedral ligand
was observed to be covalently bound to the side-chain of Ser94. The propyl
acetate ligand represents the first tetrahedral intermediate in the reaction
mechanism. Therefore, this Est30 crystal structure will help understand the mode
of action of all enzymes in the serine hydrolase superfamily.
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Selected figure(s)
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Figure 2.
Figure 2. The active site region of
Est30. (a) 2FoKFc electron density
map contoured at 1.6s. (b) Inter-
acting residues. Interatomic inter-
actions are shown in broken lines
with distances in Å . The negative
charge of the oxygen atom of the
tetrahedral intermediate and the
NH groups of Leu95 and Phe25
form an oxyanion hole (labeled in
red).
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The above figure is
reprinted
by permission from Elsevier:
J Mol Biol
(2004,
342,
551-561)
copyright 2004.
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Figure was
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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D.M.Charbonneau,
F.Meddeb-Mouelhi,
and
M.Beauregard
(2010).
A novel thermostable carboxylesterase from Geobacillus thermodenitrificans: evidence for a new carboxylesterase family.
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J Biochem,
148,
299-308.
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R.Al Khudary,
R.Venkatachalam,
M.Katzer,
S.Elleuche,
and
G.Antranikian
(2010).
A cold-adapted esterase of a novel marine isolate, Pseudoalteromonas arctica: gene cloning, enzyme purification and characterization.
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Extremophiles,
14,
273-285.
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S.Montoro-García,
I.Martínez-Martínez,
J.Navarro-Fernández,
H.Takami,
F.García-Carmona,
and
A.Sánchez-Ferrer
(2009).
Characterization of a novel thermostable carboxylesterase from Geobacillus kaustophilus HTA426 shows the existence of a new carboxylesterase family.
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J Bacteriol,
191,
3076-3085.
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D.de Pascale,
A.M.Cusano,
F.Autore,
E.Parrilli,
G.di Prisco,
G.Marino,
and
M.L.Tutino
(2008).
The cold-active Lip1 lipase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125 is a member of a new bacterial lipolytic enzyme family.
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Extremophiles,
12,
311-323.
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M.Levisson,
J.van der Oost,
and
S.W.Kengen
(2007).
Characterization and structural modeling of a new type of thermostable esterase from Thermotoga maritima.
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FEBS J,
274,
2832-2842.
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P.Liu,
H.E.Ewis,
P.C.Tai,
C.D.Lu,
and
I.T.Weber
(2007).
Crystal structure of the Geobacillus stearothermophilus carboxylesterase Est55 and its activation of prodrug CPT-11.
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J Mol Biol,
367,
212-223.
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PDB codes:
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S.Lun,
and
W.R.Bishai
(2007).
Characterization of a novel cell wall-anchored protein with carboxylesterase activity required for virulence in Mycobacterium tuberculosis.
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J Biol Chem,
282,
18348-18356.
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B.M.Liederer,
and
R.T.Borchardt
(2006).
Enzymes involved in the bioconversion of ester-based prodrugs.
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J Pharm Sci,
95,
1177-1195.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
