Family Report for: Plant_carboxylesterasePlant_carboxylesterase  Relationship Family Plant_carboxylesterase Block H
Comment No plant Carboxylesterase show the SEDCLYLN motif (prosite PS00941). These carboxylesterase are related to the Hormone sensitive lipase. Gibbereline Insensitive Dwarf1 GID1 has a primary structure similar to that of the hormone-sensitive lipase. Gibberellins (GAs) are tetracyclic, diterpenoid plant hormones, essential for many developmental processes in higher plants HSLs. The nuclear GA receptor evolved from an esterase. 2-hydroxyisoflavone dehydratase from leguminosae also belong to this family, in these particular enzymes the catalytic serine is replaced by threonine. In tulips tuliposide-converting enzyme (TCE) purified from tulip bulbs catalyzed the conversion of tuliposides to tulipalins.The lactone-forming carboxylesterases, specifically catalyzing intramolecular transesterification, but not hydrolysis
References 8 more
Rui C, Peng F, Fan Y, Zhang Y, Zhang Z, Xu N, Zhang H, Wang J, Li S and Ye W <7 more author(s)> Rui C, Peng F, Fan Y, Zhang Y, Zhang Z, Xu N, Zhang H, Wang J, Li S, Yang T, Malik WA, Lu X, Chen X, Wang D, Chen C, Gao W, Ye W (- 7) Ref: BMC Plant Biol, 22:194, 2022 : PubMed ESTHER: Rui_2022_BMC.Plant.Biol_22_194 PubMedSearch: Rui 2022 BMC.Plant.Biol 22 194 PubMedID: 35413814 Abstract BACKGROUND: Carboxylesterase (CXE) is a type of hydrolase with alpha/beta sheet hydrolase activity widely found in animals, plants and microorganisms, which plays an important role in plant growth, development and resistance to stress. RESULTS: A total of 72, 74, 39, 38 CXE genes were identified in Gossypium barbadense, Gossypium hirsutum, Gossypium raimondii and Gossypium arboreum, respectively. The gene structure and expression pattern were analyzed. The GBCXE genes were divided into 6 subgroups, and the chromosome distribution of members of the family were mapped. Analysis of promoter cis-acting elements showed that most GBCXE genes contain cis-elements related to plant hormones (GA, IAA) or abiotic stress. These 6 genes we screened out were expressed in the root, stem and leaf tissues. Combined with the heat map, GBCXE49 gene was selected for subcellular locate and confirmed that the protein was expressed in the cytoplasm. CONCLUSIONS: The collinearity analysis of the CXE genes of the four cotton species in this family indicated that tandem replication played an indispensable role in the evolution of the CXE gene family. The expression patterns of GBCXE gene under different stress treatments indicated that GBCXE gene may significantly participate in the response to salt and alkaline stress through different mechanisms. Through the virus-induced gene silencing technology (VIGS), it was speculated that GBCXE49 gene was involved in the response to alkaline stress in G. barbadense. Title: Molecular determinants that convert hormone sensitive lipase into gibberellin receptor Hirano K, Aya K, Matsuoka M, Ueguchi-Tanaka M Ref: Protein Pept Lett, 19:180, 2012 : PubMed ESTHER: Hirano_2012_Protein.Pept.Lett_19_180 PubMedSearch: Hirano 2012 Protein.Pept.Lett 19 180 PubMedID: 21933120 Gene_locus related to this paper: orysa-gid1 Abstract Gibberellins (GAs) are tetracyclic, diterpenoid plant hormones, essential for many developmental processes in higher plants. Plants perceive GA through a nuclear-localized GA receptor, GA INSENSITIVE DWARF1 (GID1). From sequence similarity, it is suggested that GID1 evolved from a hormone-sensitive lipase (HSL), and recent x-ray crystallography of the GA-GID1 complex has given insights into how GID1 recognizes GA. Analyses of the GA signaling pathway in several plant species further suggest that the GID1-mediated GA signaling pathway emerged in the vascular plant lineage and since then regulation of GA recognition specificity seems to have been fine tuned to strictly regulate the on-off GA signal. Title: The carboxylesterase gene family from Arabidopsis thaliana Marshall SD, Putterill JJ, Plummer KM, Newcomb RD Ref: Journal of Molecular Evolution, 57:487, 2003 : PubMed ESTHER: Marshall_2003_J.Mol.Evol_57_487 PubMedSearch: Marshall 2003 J.Mol.Evol 57 487 PubMedID: 14738307 Gene_locus related to this paper: 9rosa-CXE1, 9rosa-CXE2, 9rosa-CXE3, 9rosa-CXE4, 9rosa-CXE5, 9rosa-CXE6, 9rosa-CXE7, 9rosa-CXE8, 9rosa-CXE9, 9rosa-CXE10, 9rosa-CXE11, 9rosa-CXE12, actde-CXE1, actde-CXE3, actde-CXE4, actde-CXE5, actde-CXE6, actde-CXE7, actde-CXE8, actde-CXE9, actde-CXE10, arath-At2g45610, arath-AT2G03550, arath-AT5G27320, arath-AT5G62180, arath-CXE12, arath-CXE15, arath-F1N13.220, arath-F14J22.11, arath-F14J22.12, arath-F16N3.25, arath-CXE8, arath-At5g14310, arath-CXE6, arath-gid1, arath-GID1B, arath-CXE11, arath-CXE18, arath-Q8LF34, arath-CXE13, arath-CXE1, capan-PepEST, lyces-Q9ZWF3, nicta-hsr203j, orysa-Q7XTC5, orysa-Q852M6, orysa-Q8GSE8, orysa-Q8H5P9, orysa-Q8H5P5, orysa-Q8H5P4, orysa-Q7F1Y5, orysa-Q8GS14, orysa-Q8GSJ3, orysa-Q8GRZ3, orysa-Q8H3K6, orysa-Q8H3K4, orysa-Q8RZ79, orysa-Q93VD4, orysa-Q94JD7, pinra-PrMC3, pissa-Q9SSY8, vitvi-BIG8.1 Abstract Carboxylesterases hydrolyze esters of short-chain fatty acids and have roles in animals ranging from signal transduction to xenobiotic detoxification. In plants, however, little is known of their roles. We have systematically mined the genome from the model plant Arabidopsis thaliana for carboxylesterase genes and studied their distribution in the genome and expression profile across a range of tissues. Twenty carboxylesterase genes (AtCXE) were identified. The AtCXE family shares conserved sequence motifs and secondary structure characteristics with carboxylesterases and other members of the larger alpha/beta hydrolase fold superfamily of enzymes. Phylogenetic analysis of the AtCXE genes together with other plant carboxylesterases distinguishes seven distinct clades, with an Arabidopsis thaliana gene represented in six of the seven clades. The AtCXE genes are widely distributed across the genome (present in four of five chromosomes), with the exception of three clusters of tandemly duplicated genes. Of the interchromosomal duplication events, two have been mediated through newly identified partial chromosomal duplication events that also include other genes surrounding the AtCXE loci. Eighteen of the 20 AtCXE genes are expressed over a broad range of tissues, while the remaining 2 (unrelated) genes are expressed only in the flowers and siliques. Finally, hypotheses for the functional roles of the AtCXE family members are presented based on the phylogenetic relationships with other plant carboxylesterases of known function, their expression profile, and knowledge of likely esterase substrates found in plants. 8 less Other Papers
Rui C, Peng F, Fan Y, Zhang Y, Zhang Z, Xu N, Zhang H, Wang J, Li S and Ye W <7 more author(s)> Rui C, Peng F, Fan Y, Zhang Y, Zhang Z, Xu N, Zhang H, Wang J, Li S, Yang T, Malik WA, Lu X, Chen X, Wang D, Chen C, Gao W, Ye W (- 7) Ref: BMC Plant Biol, 22:194, 2022 : PubMed ESTHER: Rui_2022_BMC.Plant.Biol_22_194 PubMedSearch: Rui 2022 BMC.Plant.Biol 22 194 PubMedID: 35413814 Abstract BACKGROUND: Carboxylesterase (CXE) is a type of hydrolase with alpha/beta sheet hydrolase activity widely found in animals, plants and microorganisms, which plays an important role in plant growth, development and resistance to stress. RESULTS: A total of 72, 74, 39, 38 CXE genes were identified in Gossypium barbadense, Gossypium hirsutum, Gossypium raimondii and Gossypium arboreum, respectively. The gene structure and expression pattern were analyzed. The GBCXE genes were divided into 6 subgroups, and the chromosome distribution of members of the family were mapped. Analysis of promoter cis-acting elements showed that most GBCXE genes contain cis-elements related to plant hormones (GA, IAA) or abiotic stress. These 6 genes we screened out were expressed in the root, stem and leaf tissues. Combined with the heat map, GBCXE49 gene was selected for subcellular locate and confirmed that the protein was expressed in the cytoplasm. CONCLUSIONS: The collinearity analysis of the CXE genes of the four cotton species in this family indicated that tandem replication played an indispensable role in the evolution of the CXE gene family. The expression patterns of GBCXE gene under different stress treatments indicated that GBCXE gene may significantly participate in the response to salt and alkaline stress through different mechanisms. Through the virus-induced gene silencing technology (VIGS), it was speculated that GBCXE49 gene was involved in the response to alkaline stress in G. barbadense. Title: Evolution and diversification of the plant gibberellin receptor GID1 Yoshida H, Tanimoto E, Hirai T, Miyanoiri Y, Mitani R, Kawamura M, Takeda M, Takehara S, Hirano K and Ueguchi-Tanaka M <3 more author(s)> Yoshida H, Tanimoto E, Hirai T, Miyanoiri Y, Mitani R, Kawamura M, Takeda M, Takehara S, Hirano K, Kainosho M, Akagi T, Matsuoka M, Ueguchi-Tanaka M (- 3) Ref: Proc Natl Acad Sci U S A, 115:E7844, 2018 : PubMed ESTHER: Yoshida_2018_Proc.Natl.Acad.Sci.U.S.A_115_E7844 PubMedSearch: Yoshida 2018 Proc.Natl.Acad.Sci.U.S.A 115 E7844 PubMedID: 30068603 Abstract The plant gibberellin (GA) receptor GID1 shows sequence similarity to carboxylesterase (CXE). Here, we report the molecular evolution of GID1 from establishment to functionally diverse forms in eudicots. By introducing 18 mutagenized rice GID1s into a rice gid1 null mutant, we identified the amino acids crucial for GID1 activity in planta. We focused on two amino acids facing the C2/C3 positions of ent-gibberellane, not shared by lycophytes and euphyllophytes, and found that adjustment of these residues resulted in increased GID1 affinity toward GA4, new acceptance of GA1 and GA3 carrying C13-OH as bioactive ligands, and elimination of inactive GAs. These residues rendered the GA perception system more sophisticated. We conducted phylogenetic analysis of 169 GID1s from 66 plant species and found that, unlike other taxa, nearly all eudicots contain two types of GID1, named A- and B-type. Certain B-type GID1s showed a unique evolutionary characteristic of significantly higher nonsynonymous-to-synonymous divergence in the region determining GA4 affinity. Furthermore, these B-type GID1s were preferentially expressed in the roots of Arabidopsis, soybean, and lettuce and might be involved in root elongation without shoot elongation for adaptive growth under low-temperature stress. Based on these observations, we discuss the establishment and adaption of GID1s during plant evolution. Title: Molecular identification of tuliposide B-converting enzyme: a lactone-forming carboxylesterase from the pollen of tulip Nomura T, Murase T, Ogita S, Kato Y Ref: Plant J, 83:252, 2015 : PubMed ESTHER: Nomura_2015_Plant.J_83_252 PubMedSearch: Nomura 2015 Plant.J 83 252 PubMedID: 25997073 Gene_locus related to this paper: tulge-a0a0h5bmx5 Abstract 6-Tuliposides A (PosA) and B (PosB), which are the major secondary metabolites in tulip (Tulipa gesneriana), are enzymatically converted to the antimicrobial lactonized aglycons, tulipalins A (PaA) and B (PaB), respectively. We recently identified a PosA-converting enzyme (TCEA) as the first reported member of the lactone-forming carboxylesterases. Herein, we describe the identification of another lactone-forming carboxylesterase, PosB-converting enzyme (TCEB), which preferentially reacts with PosB to give PaB. This enzyme was isolated from tulip pollen, which showed high PosB-converting activity. Purified TCEB exhibited greater activity towards PosB than PosA, which was contrary to that of the TCEA. Novel cDNA (TgTCEB1) encoding the TCEB was isolated from tulip pollen. TgTCEB1 belonged to the carboxylesterase family and was approximately 50% identical to the TgTCEA polypeptides. Functional characterization of the recombinant enzyme verified that TgTCEB1 catalyzed the conversion of PosB to PaB with an activity comparable with the native TCEB. RT-qPCR analysis of each part of plant revealed that TgTCEB1 transcripts were limited almost exclusively to the pollen. Furthermore, the immunostaining of the anther cross-section using anti-TgTCEB1 polyclonal antibody verified that TgTCEB1 was specifically expressed in the pollen grains, but not in the anther cells. N-terminal transit peptide of TgTCEB1 was shown to function as plastid-targeted signal. Taken together, these results indicate that mature TgTCEB1 is specifically localized in plastids of pollen grains. Interestingly, PosB, the substrate of TgTCEB1, accumulated on the pollen surface, but not in the intracellular spaces of pollen grains. Title: Molecular diversity of tuliposide A-converting enzyme in the tulip Nomura T, Tsuchigami A, Ogita S, Kato Y Ref: Biosci Biotechnol Biochem, 77:1042, 2013 : PubMed ESTHER: Nomura_2013_Biosci.Biotechnol.Biochem_77_1042 PubMedSearch: Nomura 2013 Biosci.Biotechnol.Biochem 77 1042 PubMedID: 23649245 Gene_locus related to this paper: tulge-tcab2, tulge-tcab1, tulge-tcab3, tulge-tcab4 Abstract Tuliposide A-converting enzyme (TCEA) catalyzes the conversion of 6-tuliposide A to its lactonized aglycon, tulipalin A, in the tulip (Tulipa gesneriana). The TgTCEA gene, isolated previously from petals, was transcribed in all tulip tissues but not in the bulbs despite the presence of TCEA activity, which allowed prediction of the presence of a TgTCEA isozyme gene preferentially expressed in the bulbs. Here, the TgTCEA-b gene, the TgTCEA homolog, was identified in bulbs. TgTCEA-b polypeptides showed approximately 77% identity to the petal TgTCEA. Functional characterization of the recombinant enzyme verified that TgTCEA-b encoded the TCEA. Moreover, the TgTCEA-b was found to be localized to plastids, as found for the petal TgTCEA. Transcript analysis revealed that TgTCEA-b was functionally transcribed in the bulb scales, unlike the TgTCEA gene, whose transcripts were absent there. In contrast, TgTCEA-b transcripts were in the minority in other tissues where TgTCEA transcripts were dominant, indicating a tissue preference for the transcription of those isozyme genes. Title: Molecular determinants that convert hormone sensitive lipase into gibberellin receptor Hirano K, Aya K, Matsuoka M, Ueguchi-Tanaka M Ref: Protein Pept Lett, 19:180, 2012 : PubMed ESTHER: Hirano_2012_Protein.Pept.Lett_19_180 PubMedSearch: Hirano 2012 Protein.Pept.Lett 19 180 PubMedID: 21933120 Gene_locus related to this paper: orysa-gid1 Abstract Gibberellins (GAs) are tetracyclic, diterpenoid plant hormones, essential for many developmental processes in higher plants. Plants perceive GA through a nuclear-localized GA receptor, GA INSENSITIVE DWARF1 (GID1). From sequence similarity, it is suggested that GID1 evolved from a hormone-sensitive lipase (HSL), and recent x-ray crystallography of the GA-GID1 complex has given insights into how GID1 recognizes GA. Analyses of the GA signaling pathway in several plant species further suggest that the GID1-mediated GA signaling pathway emerged in the vascular plant lineage and since then regulation of GA recognition specificity seems to have been fine tuned to strictly regulate the on-off GA signal. Title: A novel lactone-forming carboxylesterase: molecular identification of a tuliposide A-converting enzyme in tulip Nomura T, Ogita S, Kato Y Ref: Plant Physiol, 159:565, 2012 : PubMed ESTHER: Nomura_2012_Plant.Physiol_159_565 PubMedSearch: Nomura 2012 Plant.Physiol 159 565 PubMedID: 22474185 Gene_locus related to this paper: tulge-tcea1, tulge-tcea2 Abstract Tuliposides, the glucose esters of 4-hydroxy-2-methylenebutanoate and 3,4-dihydroxy-2-methylenebutanoate, are major secondary metabolites in tulip (Tulipa gesneriana). Their lactonized aglycons, tulipalins, function as defensive chemicals due to their biological activities. We recently found that tuliposide-converting enzyme (TCE) purified from tulip bulbs catalyzed the conversion of tuliposides to tulipalins, but the possibility of the presence of several TCE isozymes was raised: TCE in tissues other than bulbs is different from bulb TCE. Here, to prove this hypothesis, TCE was purified from petals, which have the second highest TCE activity after bulbs. The purified enzyme, like the bulb enzyme, preferentially accepted tuliposides as substrates, with 6-tuliposide A the best substrate, which allowed naming the enzyme tuliposide A-converting enzyme (TCEA), but specific activity and molecular mass differed between the petal and bulb enzymes. After peptide sequencing, a novel cDNA (TgTCEA) encoding petal TCEA was isolated, and the functional characterization of the recombinant enzyme verified that TgTCEA catalyzes the conversion of 6-tuliposide A to tulipalin A. TgTCEA was transcribed in all tulip tissues but not in bulbs, indicating the presence of a bulb-specific TgTCEA, as suggested by the distinct enzymatic characters between the petal and bulb enzymes. Plastidial localization of TgTCEA enzyme was revealed, which allowed proposing a cytological mechanism of TgTCE-mediated tulipalin formation in the tulip defensive strategy. Site-directed mutagenesis of TgTCEA suggested that the oxyanion hole and catalytic triad characteristic of typical carboxylesterases are essential for the catalytic process of TgTCEA enzyme. To our knowledge, TgTCEA is the first identified member of the lactone-forming carboxylesterases, specifically catalyzing intramolecular transesterification. Title: Gibberellin-induced DELLA recognition by the gibberellin receptor GID1 Murase K, Hirano Y, Sun TP, Hakoshima T Ref: Nature, 456:459, 2008 : PubMed ESTHER: Murase_2008_Nature_456_459 PubMedSearch: Murase 2008 Nature 456 459 PubMedID: 19037309 Gene_locus related to this paper: arath-GID1B Abstract Gibberellins control a range of growth and developmental processes in higher plants and have been widely used in the agricultural industry. By binding to a nuclear receptor, GIBBERELLIN INSENSITIVE DWARF1 (GID1), gibberellins regulate gene expression by promoting degradation of the transcriptional regulator DELLA proteins, including GIBBERELLIN INSENSITIVE (GAI). The precise manner in which GID1 discriminates and becomes activated by bioactive gibberellins for specific binding to DELLA proteins remains unclear. Here we present the crystal structure of a ternary complex of Arabidopsis thaliana GID1A, a bioactive gibberellin and the amino-terminal DELLA domain of GAI. In this complex, GID1A occludes gibberellin in a deep binding pocket covered by its N-terminal helical switch region, which in turn interacts with the DELLA domain containing DELLA, VHYNP and LExLE motifs. Our results establish a structural model of a plant hormone receptor that is distinct from the mechanism of the hormone perception and effector recognition of the known auxin receptors. Title: Structural basis for gibberellin recognition by its receptor GID1 Shimada A, Ueguchi-Tanaka M, Nakatsu T, Nakajima M, Naoe Y, Ohmiya H, Kato H, Matsuoka M Ref: Nature, 456:520, 2008 : PubMed ESTHER: Shimada_2008_Nature_456_520 PubMedSearch: Shimada 2008 Nature 456 520 PubMedID: 19037316 Gene_locus related to this paper: orysa-gid1 Abstract Gibberellins (GAs) are phytohormones essential for many developmental processes in plants. A nuclear GA receptor, GIBBERELLIN INSENSITIVE DWARF1 (GID1), has a primary structure similar to that of the hormone-sensitive lipases (HSLs). Here we analyse the crystal structure of Oryza sativa GID1 (OsGID1) bound with GA(4) and GA(3) at 1.9 A resolution. The overall structure of both complexes shows an alpha/beta-hydrolase fold similar to that of HSLs except for an amino-terminal lid. The GA-binding pocket corresponds to the substrate-binding site of HSLs. On the basis of the OsGID1 structure, we mutagenized important residues for GA binding and examined their binding activities. Almost all of them showed very little or no activity, confirming that the residues revealed by structural analysis are important for GA binding. The replacement of Ile 133 with Leu or Val-residues corresponding to those of the lycophyte Selaginella moellendorffii GID1s-caused an increase in the binding affinity for GA(34), a 2beta-hydroxylated GA(4). These observations indicate that GID1 originated from HSL and was further modified to have higher affinity and more strict selectivity for bioactive GAs by adapting the amino acids involved in GA binding in the course of plant evolution. Title: High-resolution crystal structure of plant carboxylesterase AeCXE1, from Actinidia eriantha, and its complex with a high-affinity inhibitor paraoxon Ileperuma NR, Marshall SD, Squire CJ, Baker HM, Oakeshott JG, Russell RJ, Plummer KM, Newcomb RD, Baker EN Ref: Biochemistry, 46:1851, 2007 : PubMed ESTHER: Ileperuma_2007_Biochemistry_46_1851 PubMedSearch: Ileperuma 2007 Biochemistry 46 1851 PubMedID: 17256879 Gene_locus related to this paper: actde-CXE1 Inhibitor(s) related to this paper: Dimethyl-phosphorochloridate, Paraoxon Abstract Carboxylesterases (CXEs) are widely distributed in plants, where they have been implicated in roles that include plant defense, plant development, and secondary metabolism. We have cloned, overexpressed, purified, and crystallized a carboxylesterase from the kiwifruit species Actinidia eriantha (AeCXE1). The structure of AeCXE1 was determined by X-ray crystallography at 1.4 A resolution. The crystal structure revealed that AeCXE1 is a member of the alpha/beta-hydrolase fold superfamily, most closely related structurally to the hormone-sensitive lipase subgroup. The active site of the enzyme, located in an 11 A deep hydrophobic gorge, contains the conserved catalytic triad residues Ser169, Asp276, and His306. Kinetic analysis using artificial ester substrates showed that the enzyme can hydrolyze a range of carboxylester substrates with acyl groups ranging from C2 to C16, with a preference for butyryl moieties. This preference was supported by the discovery of a three-carbon acyl adduct bound to the active site Ser169 in the native structure. AeCXE1 was also found to be inhibited by organophosphates, with paraoxon (IC50 = 1.1 muM) a more potent inhibitor than dimethylchlorophosphate (DMCP; IC50 = 9.2 muM). The structure of AeCXE1 with paraoxon bound was determined at 2.3 A resolution and revealed that the inhibitor binds covalently to the catalytic serine residue, with virtually no change in the structure of the enzyme. The structural information for AeCXE1 provides a basis for addressing the wider functional roles of carboxylesterases in plants. Title: Molecular and biochemical characterization of 2-hydroxyisoflavanone dehydratase. Involvement of carboxylesterase-like proteins in leguminous isoflavone biosynthesis Akashi T, Aoki T, Ayabe S Ref: Plant Physiol, 137:882, 2005 : PubMed ESTHER: Akashi_2005_Plant.Physiol_137_882 PubMedSearch: Akashi 2005 Plant.Physiol 137 882 PubMedID: 15734910 Gene_locus related to this paper: glyec-q5nuf4, soybn-q5nuf3 Abstract Isoflavonoids are ecophysiologically active secondary metabolites of the Leguminosae and known for health-promoting phytoestrogenic functions. Isoflavones are synthesized by 1,2-elimination of water from 2-hydroxyisoflavanones, the first intermediate with the isoflavonoid skeleton, but details of this dehydration have been unclear. We screened the extracts of repeatedly fractionated Escherichia coli expressing a Glycyrrhiza echinata cDNA library for the activity to convert a radiolabeled precursor into formononetin (7-hydroxy-4'-methoxyisoflavone), and a clone of 2-hydroxyisoflavanone dehydratase (HID) was isolated. Another HID cDNA was cloned from soybean (Glycine max), based on the sequence information in its expressed sequence tag library. Kinetic studies revealed that G. echinata HID is specific to 2,7-dihydroxy-4'-methoxyisoflavanone, while soybean HID has broader specificity to both 4'-hydroxylated and 4'-methoxylated 2-hydroxyisoflavanones, reflecting the structures of isoflavones contained in each plant species. Strikingly, HID proteins were members of a large carboxylesterase family, of which plant proteins form a monophyletic group and some are assigned defensive functions with no intrinsic catalytic activities identified. Site-directed mutagenesis with soybean HID protein suggested that the characteristic oxyanion hole and catalytic triad are essential for the dehydratase as well as the faint esterase activities. The findings, to our knowledge, represent a new example of recruitment of enzymes of primary metabolism during the molecular evolution of plant secondary metabolism. Title: The carboxylesterase gene family from Arabidopsis thaliana Marshall SD, Putterill JJ, Plummer KM, Newcomb RD Ref: Journal of Molecular Evolution, 57:487, 2003 : PubMed ESTHER: Marshall_2003_J.Mol.Evol_57_487 PubMedSearch: Marshall 2003 J.Mol.Evol 57 487 PubMedID: 14738307 Gene_locus related to this paper: 9rosa-CXE1, 9rosa-CXE2, 9rosa-CXE3, 9rosa-CXE4, 9rosa-CXE5, 9rosa-CXE6, 9rosa-CXE7, 9rosa-CXE8, 9rosa-CXE9, 9rosa-CXE10, 9rosa-CXE11, 9rosa-CXE12, actde-CXE1, actde-CXE3, actde-CXE4, actde-CXE5, actde-CXE6, actde-CXE7, actde-CXE8, actde-CXE9, actde-CXE10, arath-At2g45610, arath-AT2G03550, arath-AT5G27320, arath-AT5G62180, arath-CXE12, arath-CXE15, arath-F1N13.220, arath-F14J22.11, arath-F14J22.12, arath-F16N3.25, arath-CXE8, arath-At5g14310, arath-CXE6, arath-gid1, arath-GID1B, arath-CXE11, arath-CXE18, arath-Q8LF34, arath-CXE13, arath-CXE1, capan-PepEST, lyces-Q9ZWF3, nicta-hsr203j, orysa-Q7XTC5, orysa-Q852M6, orysa-Q8GSE8, orysa-Q8H5P9, orysa-Q8H5P5, orysa-Q8H5P4, orysa-Q7F1Y5, orysa-Q8GS14, orysa-Q8GSJ3, orysa-Q8GRZ3, orysa-Q8H3K6, orysa-Q8H3K4, orysa-Q8RZ79, orysa-Q93VD4, orysa-Q94JD7, pinra-PrMC3, pissa-Q9SSY8, vitvi-BIG8.1 Abstract Carboxylesterases hydrolyze esters of short-chain fatty acids and have roles in animals ranging from signal transduction to xenobiotic detoxification. In plants, however, little is known of their roles. We have systematically mined the genome from the model plant Arabidopsis thaliana for carboxylesterase genes and studied their distribution in the genome and expression profile across a range of tissues. Twenty carboxylesterase genes (AtCXE) were identified. The AtCXE family shares conserved sequence motifs and secondary structure characteristics with carboxylesterases and other members of the larger alpha/beta hydrolase fold superfamily of enzymes. Phylogenetic analysis of the AtCXE genes together with other plant carboxylesterases distinguishes seven distinct clades, with an Arabidopsis thaliana gene represented in six of the seven clades. The AtCXE genes are widely distributed across the genome (present in four of five chromosomes), with the exception of three clusters of tandemly duplicated genes. Of the interchromosomal duplication events, two have been mediated through newly identified partial chromosomal duplication events that also include other genes surrounding the AtCXE loci. Eighteen of the 20 AtCXE genes are expressed over a broad range of tissues, while the remaining 2 (unrelated) genes are expressed only in the flowers and siliques. Finally, hypotheses for the functional roles of the AtCXE family members are presented based on the phylogenetic relationships with other plant carboxylesterases of known function, their expression profile, and knowledge of likely esterase substrates found in plants. No structure scheme yet for this family
Structures in Plant_carboxylesterase family (11)
Genes Proteins in Plant_carboxylesterase family (545)
Fragments of genes in Plant_carboxylesterase family (46)
Substrates of some enzymes in the Plant_carboxylesterase family (28)
Inhibitors of some enzymes in the Plant_carboxylesterase family (3)
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