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1. Full Text The role of protein dynamics in the evolution of new enzyme function
by Campbell, Eleanor and Kaltenbach, Miriam and Correy, Galen J and Carr, Paul D and Porebski, Benjamin T and Livingstone, Emma K and Afriat-Jurnou, Livnat and Buckle, Ashley M and Weik, Martin and Hollfelder, Florian and Tokuriki, Nobuhiko and Jackson, Colin J
Nature Chemical Biology, ISSN 1552-4450, 11/2016, Volume 12, Issue 11, pp. 944 - 950
Enzymes must be ordered to allow the stabilization of transition states by their active sites, yet dynamic enough to adopt alternative conformations suited to... 
EVOLVABILITY | CATALYSIS | MOLECULAR-DYNAMICS | DESIGN | BIOCHEMISTRY & MOLECULAR BIOLOGY | ALGORITHM | COMPUTER-SIMULATIONS | NETWORKS | BACTERIAL PHOSPHOTRIESTERASE | EPISTASIS | CONFORMATIONAL DIVERSITY | Biocatalysis | Pseudomonas - enzymology | Carboxylic Ester Hydrolases - chemistry | Phosphoric Triester Hydrolases - metabolism | Protein Conformation | Phosphoric Triester Hydrolases - chemistry | Carboxylic Ester Hydrolases - metabolism | Evolution, Molecular | Enzymes | Biophysics | Crystallography | Proteomics
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2. Full Text Characterization of a New Metallo-beta-Lactamase Gene, bla(NDM-1), and a Novel Erythromycin Esterase Gene Carried on a Unique Genetic Structure in Klebsiella pneumoniae Sequence Type 14 from India
by Yong, D and Toleman, MA and Giske, CG and Cho, HS and Sundman, K and Lee, K and Walsh, TR
ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, ISSN 0066-4804, 12/2009, Volume 53, Issue 12, pp. 5046 - 5054
A Swedish patient of Indian origin traveled to New Delhi, India, and acquired a urinary tract infection caused by a carbapenem-resistant Klebsiella pneumoniae... 
BACTERIA | ISCR ELEMENTS | PSEUDOMONAS-AERUGINOSA | ANTIBIOTIC-RESISTANCE | MEDIATED RIFAMPIN RESISTANCE | CARBAPENEMASES | MICROBIOLOGY | PHARMACOLOGY & PHARMACY | MULTIDRUG-RESISTANCE | STREPTOGRAMIN | BLOOD-STREAM INFECTIONS | CLINICAL ISOLATE | Klebsiella pneumoniae - drug effects | Carboxylic Ester Hydrolases - chemistry | Carboxylic Ester Hydrolases - classification | Humans | Cefotaxime - metabolism | Molecular Sequence Data | Cefuroxime - metabolism | Cefuroxime - pharmacology | Microbial Sensitivity Tests | beta-Lactamases - genetics | Penicillins - metabolism | Klebsiella pneumoniae - genetics | Carboxylic Ester Hydrolases - genetics | Penicillins - pharmacology | Cephalosporins - pharmacology | Amino Acid Sequence | Drug Resistance, Multiple, Bacterial - physiology | Cephalothin - pharmacology | Cephalothin - metabolism | Anti-Bacterial Agents - metabolism | Klebsiella Infections - microbiology | Electrophoresis, Gel, Pulsed-Field | Sequence Analysis, DNA | India | Sequence Homology, Amino Acid | beta-Lactamases - chemistry | beta-Lactamases - classification | Klebsiella pneumoniae - enzymology | Cefotaxime - pharmacology | Anti-Bacterial Agents - pharmacology | Kinetics | Drug Resistance, Multiple, Bacterial - genetics | Cephalosporins - metabolism
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3. Full Text A ratiometric fluorescent system for carboxylesterase detection with AIE dots as FRET donors
by Wu, Yinglong and Huang, Shuailing and Zeng, Fang and Wang, Jun and Yu, Changmin and Huang, Jing and Xie, Huiting and Wu, Shuizhu
Chemical Communications, ISSN 1359-7345, 08/2015, Volume 51, Issue 64, pp. 12791 - 12794
A ratiometric fluorescent system for CaE detection with AIE dots as the FRET donors was designed. Upon enzymatic reaction, electrostatic interaction between... 
NANOPARTICLES | MERCURY | FLUOROGENIC PROBE | AGGREGATION-INDUCED EMISSION | PH | SENSOR | CHEMISTRY, MULTIDISCIPLINARY | Fluorescent Dyes - chemistry | Carboxylic Ester Hydrolases - chemistry | Enzyme Assays - methods | Fluorescence Resonance Energy Transfer - methods | Fluorescein - chemistry | Static Electricity | Carboxylic Ester Hydrolases - metabolism
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4. Full Text Long-acting cocaine hydrolase for addiction therapy
by Xiabin Chen and Liu Xue and Shurong Hou and Zhenyu Jin and Ting Zhang and Fang Zheng and Chang-Guo Zhan
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 1/2016, Volume 113, Issue 2, pp. 422 - 427
Cocaine abuse is a world-wide public health and social problem without a US Food and Drug Administration-approved medication. An ideal anticocaine medication... 
Drug abuse | Protein engineering | Cocaine addiction | Enzyme therapy | enzyme therapy | DETOXIFICATION | DESIGN | MULTIDISCIPLINARY SCIENCES | MUTATED BUTYRYLCHOLINESTERASE | RATS | HUMAN BUTYRYLCHOLINESTERASE | MODEL | cocaine addiction | protein engineering | CATALYTIC ANTIBODY | MUTANTS | drug abuse | Cocaine - metabolism | Biocatalysis | Carboxylic Ester Hydrolases - chemistry | Carboxylic Ester Hydrolases - toxicity | Humans | Receptors, Fc - metabolism | Models, Molecular | Rats, Sprague-Dawley | Carboxylic Ester Hydrolases - administration & dosage | Hydrolysis | Animals | Time Factors | Carboxylic Ester Hydrolases - therapeutic use | Cocaine-Related Disorders - drug therapy | Mice | Enzymes | Usage | Care and treatment | Hydrolases | Cocaine | Health aspects | Methods | Index Medicus | Biological Sciences
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5. Full Text Caffeoyl Shikimate Esterase (CSE) Is an Enzyme in the Lignin Biosynthetic Pathway in Arabidopsis
by Ruben Vanholme and Igor Cesarino and Katarzyna Rataj and Yuguo Xiao and Lisa Sundin and Geert Goeminne and Hoon Kim and Joanna Cross and Kris Morreel and Pedro Araujo and Lydia Welsh and Jurgen Haustraete and Christopher McClellan and Bartel Vanholme and John Ralph and Gordon G. Simpson and Claire Halpin and Wout Boerjan and Great Lakes Bioenergy Research Center (GLBRC)
Science, ISSN 0036-8075, 9/2013, Volume 341, Issue 6150, pp. 1103 - 1106
Lignin is a major component of plant secondary cell walls. Here we describe caffeoyl shikimate esterase (CSE) as an enzyme central to the lignin biosynthetic... 
Lignin | Enzymes | Lignification | Cell walls | REPORTS | Hematocrit | Biosynthesis | Plants | Biochemical pathways | Biofuels | Research universities | TRANSCRIPTION FACTORS | ACID | THALIANA | DEPOSITION | MULTIDISCIPLINARY SCIENCES | SECONDARY CELL-WALL | PHENYLPROPANOID METABOLISM | 3'-HYDROXYLASE | GROWTH | PHENOTYPE | MONOLIGNOL BIOSYNTHESIS | Arabidopsis - genetics | Shikimic Acid - chemistry | Arabidopsis Proteins - genetics | Arabidopsis - enzymology | Lignin - biosynthesis | Arabidopsis Proteins - chemistry | Carboxylic Ester Hydrolases - chemistry | Metabolic Networks and Pathways | Glucose - chemistry | Substrate Specificity | Carboxylic Ester Hydrolases - genetics | Mutation | Arabidopsis thaliana | Physiological aspects | Genetic aspects | Flowers & plants | Wood | Polymers | Chemists | Pathways | Plants (organisms) | Esterases | Glucose | Biomass | Walls
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6. Full Text A functional peptidyl-tRNA hydrolase, ICT1, has been recruited into the human mitochondrial ribosome
by Richter, R and Rorbach, J and Pajak, A and Smith, P.M and Wessels, H.J and Huynen, M.A and Smeitink, J.A.M and Lightowlers, R.N and Chrzanowska-Lightowlers, Z.M
The EMBO Journal, ISSN 0261-4189, 2010, Volume 29, Issue 6, pp. 1116 - 1125
Bioinformatic analysis classifies the human protein encoded by immature colon carcinoma transcript-1 (ICT1) as one of a family of four putative mitochondrial... 
mitoribosomes | peptidyl‐tRNA hydrolase | translation release factor | Mitoribosomes | Peptidyl-tRNA hydrolase | Translation release factor | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | HYDROLYSIS | TRANSLATION | CELL BIOLOGY | IN-VITRO | CODONS | MESSENGER-RNA | PROTEIN-BIOSYNTHESIS | ELONGATION | peptidyl-tRNA hydrolase | TERMINATION | PROTEOMICS | Amino Acid Sequence | Carboxylic Ester Hydrolases - chemistry | Peptide Termination Factors - genetics | Humans | Molecular Sequence Data | Ribosomes - metabolism | Mitochondria - metabolism | Mitochondrial Proteins - genetics | Peptide Termination Factors - metabolism | Hydrolysis | Proteins - genetics | Proteins - metabolism | Mitochondrial Proteins - metabolism | Protein Conformation | Carboxylic Ester Hydrolases - genetics | HeLa Cells | Proteins - chemistry | Carboxylic Ester Hydrolases - metabolism | Proteins | Mutation | Molecular biology | Chemical synthesis | Bioinformatics
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7. Full Text New insights into pectin methylesterase structure and function
by Pelloux, Jérôme and Rustérucci, Christine and Mellerowicz, Ewa J and Sveriges lantbruksuniversitet
Trends in Plant Science, ISSN 1360-1385, 2007, Volume 12, Issue 6, pp. 267 - 277
In bacteria, fungi and plants, pectin methylesterases are ubiquitous enzymes that modify the degree of methylesterification of pectins, which are major... 
FIG FICUS-AWKEOTSANG | DEGRADING ENZYMES | POLLEN-TUBE GROWTH | CELL-WALL METABOLISM | GENE-EXPRESSION | ARABIDOPSIS POLLEN | METHYL ESTERASE | POLYSACCHARIDE COMPOSITION | SOLANUM-TUBEROSUM | DISEASE RESISTANCE | PLANT SCIENCES | Carboxylic Ester Hydrolases - chemistry | Cell Wall - enzymology | Gene Expression Regulation, Enzymologic | Plant Proteins - genetics | Animals | Plant Diseases - virology | Models, Biological | Plant Proteins - chemistry | Cell Wall - metabolism | Gene Expression Regulation, Plant | Plant Diseases - genetics | Protein Conformation | Carboxylic Ester Hydrolases - genetics | Plant Proteins - metabolism | Plant Diseases - parasitology | Carboxylic Ester Hydrolases - metabolism | Skogsvetenskap | Forest Science
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8. Full Text Carboxylic ester hydrolases from hyperthermophiles
by Levisson, M and Oost, van der, J and Kengen, S.W.M
Extremophiles, ISSN 1431-0651, 2009, Volume 13, Issue 4, pp. 567 - 581
Carboxylic ester hydrolyzing enzymes constitute a large group of enzymes that are able to catalyze the hydrolysis, synthesis or transesterification of an ester... 
Biochemical properties | Hyperthermophile | Carboxylic ester hydrolase | Esterase | Classification | Review | Lipase | Structure | INDUSTRIAL APPLICATIONS | HORMONE-SENSITIVE LIPASE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | MICROBIOLOGY | PYROCOCCUS-FURIOSUS | THERMOSTABLE ESTERASE | AEROPYRUM-PERNIX K1 | ARCHAEON SULFOLOBUS-SOLFATARICUS | THERMOACIDOPHILIC ARCHAEON | THERMOTOGA-MARITIMA | THERMUS-THERMOPHILUS HB27 | Carboxylic Ester Hydrolases - physiology | Temperature | Carboxylic Ester Hydrolases - chemistry | Models, Chemical | Enzymes - physiology | Molecular Conformation | Open Reading Frames | Substrate Specificity | Hot Temperature | Archaea - enzymology | Hydrolysis | Biotechnology - methods | Esters - chemistry | Models, Biological | Bacteria - enzymology | Genome | Enzymes | Biotechnology | Bacteria | Biochemistry | crystal-structure | pyrococcus-furiosus | aeropyrum-pernix k1 | thermostable esterase | hormone-sensitive lipase | thermus-thermophilus hb27 | archaeon sulfolobus-solfataricus | thermotoga-maritima | industrial applications | thermoacidophilic archaeon
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9. Full Text Installing hydrolytic activity into a completely de novo protein framework
by Burton, Antony J and Thomson, Andrew R and Dawson, William M and Brady, R. Leo and Woolfson, Derek N
Nature Chemistry, ISSN 1755-4330, 09/2016, Volume 8, Issue 9, pp. 837 - 844
The design of enzyme-like catalysts tests our understanding of sequence-to-structure/function relationships in proteins. Here we install hydrolytic activity... 
Hydrolysis | Protein Structure, Tertiary | Protein Conformation, alpha-Helical | Catalytic Domain | Carboxylic Ester Hydrolases - chemistry | Protein Engineering - methods | Carboxylic Ester Hydrolases - genetics | Catalysis | Kinetics | Mutation | Nitrophenols - chemistry
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10. Full Text Molecular Engineering of Organophosphate Hydrolysis Activity from a Weak Promiscuous Lactonase Template
by Meier, Monika M and Rajendran, Chitra and Malisi, Christoph and Fox, Nicholas G and Xu, Chengfu and Schlee, Sandra and Barondeau, David P and Höcker, Birte and Sterner, Reinhard and Raushel, Frank M
Journal of the American Chemical Society, ISSN 0002-7863, 08/2013, Volume 135, Issue 31, pp. 11670 - 11677
Rapid evolution of enzymes provides unique molecular insights into the remarkable adaptability of proteins and helps to elucidate the relationship between... 
SITE | HYDROLASES | MUTAGENESIS | ENZYME | PHOSPHOTRIESTERASE | EVOLUTION | SUBSTRATE | DEGRADATION | VERSATILITY | TOXICITY | CHEMISTRY, MULTIDISCIPLINARY | Organophosphates - metabolism | Carboxylic Ester Hydrolases - chemistry | Phosphoric Triester Hydrolases - genetics | Stereoisomerism | Models, Molecular | Substrate Specificity | Crystallography, X-Ray | Hydrolysis | Pseudomonas - enzymology | Mutagenesis | Phosphoric Triester Hydrolases - metabolism | Protein Conformation | Carboxylic Ester Hydrolases - genetics | Phosphoric Triester Hydrolases - chemistry | Pseudomonas - chemistry | Pseudomonas - genetics | Pseudomonas - metabolism | Carboxylic Ester Hydrolases - metabolism | Measurement | Analysis | Catalysis | Research | Enzyme kinetics | Activation energy | Index Medicus
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11. Full Text Pectin methylesterase and its proteinaceous inhibitor: a review
by Jolie, Ruben P and Duvetter, Thomas and Van Loey, Ann M and Hendrickx, Marc E
Carbohydrate Research, ISSN 0008-6215, 2010, Volume 345, Issue 18, pp. 2583 - 2595
Pectin methylesterase (PME) catalyses the demethoxylation of pectin, a major plant cell wall polysaccharide. Through modification of the number and... 
Pectinesterase (PE) | Food processing | Cloud stability | Pectin methylesterase inhibitor (PMEI) | Pectin methylesterase (PME) | Interaction | MOSAIC-VIRUS MOVEMENT | POLLEN-TUBE GROWTH | ORANGE JUICE CLOUD | PECTINESTERASE INHIBITOR | BIOCHEMISTRY & MOLECULAR BIOLOGY | CHEMISTRY, ORGANIC | HIGH-PRESSURE INACTIVATION | FIG FICUS-AWKEOTSANG | METHYL ESTERASE-ACTIVITY | AMINO-ACID-SEQUENCE | CELL-WALL EXTENSION | KIWI FRUIT | CHEMISTRY, APPLIED | Plant Proteins - genetics | Carboxylic Ester Hydrolases - chemistry | Enzyme Inhibitors - metabolism | Protein Structure, Secondary | Plant Proteins - chemistry | Enzyme Inhibitors - chemistry | Plant Proteins - antagonists & inhibitors | Carboxylic Ester Hydrolases - genetics | Plant Proteins - metabolism | Carboxylic Ester Hydrolases - metabolism
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12. Full Text Structure, function and regulation of carboxylesterases
by Satoh, Tetsuo and Hosokawa, Masakiyo
Chemico-Biological Interactions, ISSN 0009-2797, 2006, Volume 162, Issue 3, pp. 195 - 211
This review covers current developments in molecular-based studies of the structure and function of carboxylesterases. To allay the confusion of the classic... 
Function | Molecular structure | Novel nomenclature and classification | Enzyme induction | Drug metabolism | Regulation | Gene expression | Carboxylesterases | HUMAN PLASMA | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRIACYLGLYCEROL HYDROLASE | MOUSE-LIVER | carboxylesterases | DI-(2-ETHYLHEXYL) PHTHALATE | RAT-LIVER MICROSOMES | molecular structure | enzyme induction | regulation | function | drug metabolism | novel nomenclature and classification | MULTIGENE FAMILY | MAMMALIAN CARBOXYLESTERASES | PHARMACOLOGY & PHARMACY | MOLECULAR-CLONING | ENDOPLASMIC-RETICULUM | TOXICOLOGY | CDNA CLONING | gene expression | Amino Acid Sequence | Carboxylic Ester Hydrolases - chemistry | Humans | Enzyme Induction | Molecular Sequence Data | Terminology as Topic | Structure-Activity Relationship | Organophosphorus Compounds - metabolism | Animals | Insecticides - metabolism | Carboxylic Ester Hydrolases - biosynthesis | Carboxylic Ester Hydrolases - genetics | Carboxylic Ester Hydrolases - metabolism | Herbicides | Synthesis | Laws, regulations and rules | Isoenzymes | Dioxin | Physiological aspects | Lipids | Universities and colleges | Xenobiotics
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