CaesCCR11 as a member of family XV of lipolytic enzymes, it has a canonical alpha/beta hydrolase fold composed of 7 beta-strands and 6 alpha-helices, the alpha/beta architecture of the cap domain, the GLSTG pentapeptide, and the formation of distinctive salt bridges
carboxylesterases are members of the alpha/beta hydrolase family, found in animals, plants, and microorganisms. EstPS1 has a single catalytic domain of the alpha/beta hydrolase family and belongs to the carboxylesterase family. And the EstPS1 carboxylesterase is an intracellular serine hydrolase that belongs to the lipase GDSL-2 family. Members of the GDSL family possess the GDSX motif (equivalent to the classical GXSXG motif of lipases/esterases), in which nucleophilic Ser is located in block I of the protein
porcine liver carboxylesterase (PLE), with the consensus sequence motif Gly-Glu-Ser-Ala-Gly in its lipolitic active site, belongs to carboxylesterase family as a serine-type esterase
the enzyme NaM1 belongs to the carbohydrate esterase 7 (CE7) family enzymes, i.e. Axe1NaM1. CE7 enzymes are intracellular enzymes that possess a unique and narrow specificity for acetylated substrates. The putative AcXE-encoding genes, Axe1NaM1 (CE7), Axe1NaM2 (CE7), and XynBNaM3-like (CE3), have 64, 69, and 59% sequence identities, respectively, to known AcXE sequences from actinobacteria and distinct domain arrangements. The Axe1 domains are encoded by nucleotides 19 to 966 and 19 to 972 of the Axe1NaM1 and Axe1NaM2 genes, respectively, and shared 46.5% sequence identity. The two genes are located on two distinct contigs. The Axe1NaM1, Axe1NaM2, and XynBNaM3-like proteins, i.e. NaM1, NaM2, and NaM3, all exhibit a Ser-His-Asp(Glu) catalytic triad and a GXSXG or GDS(L) motif typical of the CE7 or CE3 family, respectively
the enzyme NaM2 belongs to the carbohydrate esterase 7 (CE7) family enzymes. CE7 enzymes are intracellular enzymes that possess a unique and narrow specificity for acetylated substrates. The putative AcXE-encoding genes, Axe1NaM1 (CE7), Axe1NaM2 (CE7), and XynBNaM3-like (CE3), have 64, 69, and 59% sequence identities, respectively, to known AcXE sequences from actinobacteria and distinct domain arrangements. The Axe1 domains are encoded by nucleotides 19 to 966 and 19 to 972 of the Axe1NaM1 and Axe1NaM2 genes, respectively, and share 46.5% sequence identity. The two genes are located on two distinct contigs. The Axe1NaM1, Axe1NaM2, and XynBNaM3-like proteins, i.e. NaM1, NaM2, and NaM3, all exhibit a Ser-His-Asp(Glu) catalytic triad and a GXSXG or GDS(L) motif typical of the CE7 or CE3 family, respectively
the putative AcXE-encoding genes, Axe1NaM1 (CE7), Axe1NaM2 (CE7), and XynBNaM3-like (CE3), have 64, 69, and 59% sequence identities, respectively, to known AcXE sequences from actinobacteria and distinct domain arrangements. The Axe1 domains are encoded by nucleotides 19 to 966 and 19 to 972 of the Axe1NaM1 and Axe1NaM2 genes, respectively, and shared 46.5% sequence identity. The two genes are located on two distinct contigs. The Axe1NaM1, Axe1NaM2, and XynBNaM3-like proteins, i.e. NaM1, NaM2, and NaM3, all exhibit a Ser-His-Asp(Glu) catalytic triad and a GXSXG or GDS(L) motif typical of the CE7 or CE3 family, respectively
carboxylesterases are members of the alpha/beta hydrolase family, found in animals, plants, and microorganisms. EstPS1 has a single catalytic domain of the alpha/beta hydrolase family and belongs to the carboxylesterase family. And the EstPS1 carboxylesterase is an intracellular serine hydrolase that belongs to the lipase GDSL-2 family. Members of the GDSL family possess the GDSX motif (equivalent to the classical GXSXG motif of lipases/esterases), in which nucleophilic Ser is located in block I of the protein
CaesCCR11 as a member of family XV of lipolytic enzymes, it has a canonical alpha/beta hydrolase fold composed of 7 beta-strands and 6 alpha-helices, the alpha/beta architecture of the cap domain, the GLSTG pentapeptide, and the formation of distinctive salt bridges
the knockdown of CES1 with siRNA results in lower levels of hepatitis C virus replication (reduction in hepatitis C virus RNA and NS3 and NS5A proteins by 80, 50, and 75%, respectively, up to 72 h post-transfection)
methyl 1H-indole-3-carboxylate exerts inhibitory activity on the growth of wild-type roots when applied exogenously. However, the roots of Arabidopsis plants carrying T-DNA insertions in the putative MeIAA esterase gene AtMES17 displays significantly decreased sensitivity to indole-3-acetic acid methyl ester compared with wild-type roots while remaining as sensitive to free indole.3.acetic acid as wild-type roots
underexpression by knockout mutation and/or RNAi-mediated silencing of multiple AtMES genes, including AtMES1, -2, -7, and -9, compromises systemic acquired resistance in Arabidopsis and correlated with enhanced accumulation of MeSA in the systemic tissue of systemic acquired resistance-induced plants
mutation of each and both N-glycosylation sites leads to decreased levels of secreted active hCES2. The thermostability of the glycosylation mutants is decreased
carboxylesterase 1 plays a role in the metabolism of several drugs used in the treatment of common conditions, including hypertension, congestive heart failure, and diabetes mellitus
carboxylesterases are involved in lipid homeostasis, including cholesterol metabolism and transport with a proposed role in the development of atherosclerosis
carboxylesterases are involved in lipid homeostasis, including cholesterol metabolism and transport with a proposed role in the development of atherosclerosis
carboxylesterase from the chlorpyrifos-methyl-resistant strain VOSCM of Oryzaephilus surinamensis plays a role in conferring resistance to chlorpyrifos-methyl
hepatic carboxylesterase CE1 plays a significant role in CPT-11 hydrolysis even though it is up to 100fold less efficient at drug activation than intestinal carboxylesterase. The drug activation in the intestine and kidney are likely major contributors to SN-38 production in vivo
up-regulation of CES1 is observed to favor hepatitis C virus propagation implying an important role for this host cell protein. CES1 activity is observed to increase the size and density of lipid droplets, which are necessary for the maturation of very low density lipoproteins, one of the likely vehicles for hepatitis C virus release. CES1 increases triacylglycerol and cholesteryl ester levels and apolipoprotein B secretion
indole-3-acetic acid methyl ester, i.e. methyl 1H-indole-3-carboxylate, is an inactive form of indole-3-acetic acid, and the manifestations of indole-3-acetic acid methyl ester in vivo activity are due to the action of free indole-3-acetic acid that is generated from indole-3-acetic acid methyl ester upon hydrolysis by one or more plant esterases
SABP2's methyl salicylate esterase activity is required in healthy systemic tissues of infected plants to release the active defense phytohormone SA from methyl salicylate, which serves as a long-distance signal for systemic acquired resistance
carboxylesterase-1 (CE-1) is a crucial enzyme responsible for metabolism/activation/inactivation of xenobiotics (therapeutic agents, prodrugs, abused drugs, and organophosphorus nerve agents etc.) and also involved in many other biological processes. CE-1 is responsible for the methyl ester hydrolysis of cocaine
despite having high structural similarity to and sharing an identical catalytic triad with an extensively studied esterase from Pseudomonas fluorescens, wild-type enzyme Mhg from Microbacterium hydrocarbonoxydans does not show any esterase activity. Mhg, a typical alpha/beta fold hydrolase, is a gamma-lactamase (EC 3.5.2.) and also shows perhydrolase activities. But the engineered residue L233 point mutants show specific esterase activities, overview
elevated carboxylesterase activity and increased hydrolytic metabolic capacity towards lambda-cyhalothrin contributes to the lambda-cyhalothrin insensitivity in quercetin fed Helicoverpa armigera. S,S,S-Tributyl phosphorotrithioate (DEF) treatment shows a synergistic effect on lambda-cyhalothrin toxicity to quercetin-fed Helicoverpa armigera
esterase B from Sphingobium sp. SM42 exhibits de-arenethiolase activity against cephalosporin antibiotics. It is highly active against the third and first generation cephalosporins, cefoperazone and cefazolin and demonstrates a mild activity towards the third generation drugs, ceftriaxone and cefotaxime. The enzyme is one of two esterases whose genes have been isolated from the dibutyl phthalate (DBP)-degrading soil bacterium Sphingobium sp. SM42
human carboxylesterase (CES) is a key esterase involved in the metabolism and biotransformation of drugs. Hydrolysis activity in the human small intestine is predominantly mediated by CES2A1 rather than CES1A. In drug development studies, Caco-2 cells are commonly used as a model to predict drug absorption in the human small intestine. But the expression patterns of CES2A1 and CES1A in Caco-2 cells differ from those in the human small intestine
human carboxylesterase (CES) is a key esterase involved in the metabolism and biotransformation of drugs. Hydrolysis activity in the human small intestine is predominantly mediated by CES2A1 rather than CES1A. In drug development studies, Caco-2 cells are commonly used as a model to predict drug absorption in the human small intestine. But the expression patterns of CES2A1 and CES1A in Caco-2 cells differ from those in the human small intestine. Hydrolysis levels of the CES2A1-specific substrate aspirin were similar in human iPS cell-derived enterocytes and Caco-2 cells, whereas hydrolysis of the CES1A-specific substrate monoethylglycylxylidine is observed in Caco-2 cells but not in human iPS cell-derived enterocytes
human carboxylesterase 2 (hCE2) plays important roles in the oral bioavailability and treatment outcomes of ester- or amide-containing drugs or prodrugs, such as anticancer agents CPT-11 (irinotecan) and LY2334737 (gemcitabine)
human liver carboxylesterase 1 (CES1) plays a critical role in the hydrolysis of various ester- and amide-containing molecules, including active metabolites, drugs and prodrugs
isoform-specific regulation of hepatic Ces mRNA expression and activity following administration of pharmacological activators of the constitutive androstane receptor (CAR), pregnane X receptor (PXR) and nuclear factor-E2-related protein (Nrf2) to mice, overview
possible role of the enzyme in the mouse host-parasite relationship might be to ease the passage of worms through the host's blood vessels and/or in immune evasion. Immunofluorescent detection of the host-derived enzyme on adult worms
role of carboxylesterases in the hydrolysis of the post-coital contraceptive drug anordrin in humans. CES1 shows a higher activity in liver. Anordriol shows a several fold higher affinity than anordrin for cytosol estrogen receptor
role of carboxylesterases in the hydrolysis of the post-coital contraceptive drug anordrin in humans. Isozyme carboxylesterase (CES) 1 contributes more activity than isozyme CES2 in human liver. Anordriol shows a several fold higher affinity than anordrin for cytosol estrogen receptor
SexiCXE10 acts as a general odorant-degrading enzyme and may play and important role in the detection of host plants. Female Spodoptera exigua responds significantly to (Z)-3-hexenyl acetate and other 4 volatiles with 7-10 C chain length, (E)-2-hexenyl acetate, heptyl acetate, octyl acetate and (Z)-3-hexenyl butyrate
the enzyme is involved in the decomposition of the outmost layer fungal cell walls from plant pathogen Colletotrichum glocosporioides and Colletotrichum coccodes producing 1,2-dithiane-4,5-diol. This compound triggers nekrosis in the fungus and protects the Capsicum plant and fruits from the pathogens attack that cause diseases like anthracnose
the well-conserved esterase B1 gene, BdB1, mediates malathion resistance development via gene upregulation with the use of a laboratory selected malathion-resistant strain (MR) of Bactrocera dorsalis. Enzyme BdB1 probably has the function of malathion detoxification
despite having high structural similarity to and sharing an identical catalytic triad with an extensively studied esterase from Pseudomonas fluorescens, wild-type enzyme Mhg from Microbacterium hydrocarbonoxydans does not show any esterase activity. Mhg, a typical alpha/beta fold hydrolase, is a gamma-lactamase (EC 3.5.2.) and also shows perhydrolase activities. But the engineered residue L233 point mutants show specific esterase activities, overview
isoform-specific regulation of hepatic Ces mRNA expression and activity following administration of pharmacological activators of the constitutive androstane receptor (CAR), pregnane X receptor (PXR) and nuclear factor-E2-related protein (Nrf2) to mice, overview
of 14 recombinant methyl esterase proteins tested, five show preference for methyl salicylate as a substrate and display salicylate inhibition of methyl salicylate esterase activity in vitro, i.e. AtMES1, -2, -4, -7, and -9
immobilization of a recombinant enzyme from Pyrococcus furiosus (Pf2001DELTA60) by adsorption on supports of commercial origins with different degrees of hydrophobicity allows the hyperactivation of this enzyme (140% for butyl Sepabeads and 237% for octadecyl Sepabeads) and the obtainment of biocatalysts with attractive thermostability characteristics
catalytic residues of NaM1 correspond to Ser185, His304, and Asp275. Ser185 is located toward the end of a concave substrate binding pocket that extends to the S2 pocket accommodating the substrate acyl moiety. His304 bridges Ser185 and Asp275. In the presence of substrate, Asp275 polarizes His304 to deprotonate Ser185, allowing the latter to attack the carbonyl carbon of the substrate ester to initiate bond cleavage. Enzyme NaM1 exhibits the alpha/beta-hydrolase motif GXSXG (GYSQG) in loop beta6-alpha5. Structure-function analysis, overview
catalytic residues of NaM1 correspond to Ser187, His307, and Asp273. Ser187 is located toward the end of a concave substrate binding pocket that extends to the S2 pocket accommodating the substrate acyl moiety. His307 bridges Ser185 and Asp273. In the presence of substrate, Asp273 polarizes His307 to deprotonate Ser187, allowing the latter to attack the carbonyl carbon of the substrate ester to initiate bond cleavage. Enzyme NaM1 exhibits the alpha/beta-hydrolase motif GXSXG (GYSQG) in loop beta6-alpha5. Structure-function analysis, overview
development of a system to evaluate intestinal pharmacokinetics, CES expression and function in human induced pluripotent stem (iPS) cell-derived enterocytes are analyzed. CES2A1 mRNA and protein levels in human iPS cell-derived enterocytes are comparable to Caco-2 cells, whereas CES1A levels are lower in human iPS cell-derived enterocytes compared with Caco-2 cells. The expression and activity of CES isozymes in human iPS cell-derived enterocytes are more similar to the human small intestine compared with Caco-2 cells
development of a system to evaluate intestinal pharmacokinetics, CES expression and function in human induced pluripotent stem (iPS) cell-derived enterocytes are analyzed. CES2A1 mRNA and protein levels in human iPS cell-derived enterocytes are comparable to Caco-2 cells, whereas CES1A levels are lower in human iPS cell-derived enterocytes compared with Caco-2 cells. The expression and activity of CES isozymes in human iPS cell-derived enterocytes are more similar to the human small intestine compared with Caco-2 cells
enzyme FpbH contains the catalytic triad formed by Ser100, Asp213, and His239, proposed model of FpbH generated using an alpha/beta-hydrolase template from Rhodopseudomonas palustris strain CGA009, PDB ID 4psu
residues Phe100, Met147, and Tyr457 are located near the substrate-binding pocket, multi-conformer modeling of Tyr457. Kinetic analysis of the role of Tyr457 and Met147 reveals catalytic evidence for dynamic coupling
structure homology analysis, the 640-amino acid carboxylesterase (EstPS1) contains an autotransporter (AT) domain (357-640 amino acids) that strongly improves secretory expression in the heterogeneous system
structure homology analysis, the 640-amino acid carboxylesterase (EstPS1) contains an autotransporter (AT) domain (357-640 amino acids) that strongly improves secretory expression in the heterogeneous system
three-dimensional structure modeling of enzyme CaesCCR11 using the Bacillus sp. monoacyl glycerol lipase bMGL H-257 structure as template (PBD ID 3RM3)
structure homology analysis, the 640-amino acid carboxylesterase (EstPS1) contains an autotransporter (AT) domain (357-640 amino acids) that strongly improves secretory expression in the heterogeneous system
three-dimensional structure modeling of enzyme CaesCCR11 using the Bacillus sp. monoacyl glycerol lipase bMGL H-257 structure as template (PBD ID 3RM3)