@ARTICLE{Comfort20073319,
author={Comfort, D.A. and Bobrov, K.S. and Ivanen, D.R. and Shabalin, K.A. and Harris, J.M. and Kulminskaya, A.A. and Brumer, H. and Kelly, R.M.},
title={Biochemical analysis of Thermotoga maritima GH36 α-galactosidase (TmGalA) confirms the mechanistic commonality of clan GH-D glycoside hydrolases},
journal={Biochemistry},
year={2007},
volume={46},
number={11},
pages={3319-3330},
doi={10.1021/bi061521n},
note={cited By 72},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-33947433621&doi=10.1021%2fbi061521n&partnerID=40&md5=0052f204a32353c216bae321a8599fe1},
affiliation={Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, NC 27695-7905, United States; Petersburg Nuclear Physics Institute, Russian Academy of Science, Molecular and Radiation Biology Division, Gatchina, St. Petersburg 188300, Russian Federation; School of Biotechnology, Royal Institute of Technology, AlbaNova University Centre, Stockholm, Sweden},
keywords={Anomeric stereochemistry;  Glycoside hydrolase (GH);  Mechanistic commonality, Addition reactions;  Biochemistry;  Catalyst activity;  Mutagens;  pH effects;  Stereochemistry, Enzymes, 4 nitrophenylgalactoside;  alpha galactopyranoside;  alpha galactosidase;  aspartic acid;  azide;  glucopyranoside;  glycine;  glycosidase;  mutant protein;  pyranoside;  unclassified drug, amino acid substitution;  article;  catalysis;  controlled study;  enzyme activity;  enzyme analysis;  enzyme kinetics;  enzyme mechanism;  enzyme structure;  hydrolysis;  nonhuman;  pH;  priority journal;  protein family;  site directed mutagenesis;  stereochemistry;  Thermotoga maritima, alpha-Galactosidase;  Amino Acid Sequence;  Azides;  Catalysis;  Cloning, Molecular;  Heat;  Hydrogen-Ion Concentration;  Kinetics;  Models, Molecular;  Molecular Sequence Data;  Mutagenesis, Site-Directed;  Protein Denaturation;  Sequence Alignment;  Substrate Specificity;  Thermotoga maritima, Thermotoga maritima},
chemicals_cas={4 nitrophenylgalactoside, 3150-24-1; alpha galactosidase, 9023-01-2; aspartic acid, 56-84-8, 6899-03-2; azide, 12596-60-0, 14343-69-2; glycine, 56-40-6, 6000-43-7, 6000-44-8; glycosidase, 9032-92-2; Azides; alpha-Galactosidase, 3.2.1.22},
correspondence_address1={Kelly, R.M.; Department of Chemical and Biomolecular Engineering, , Raleigh, NC 27695-7905, United States; email: rmkelly@eos.ncsu.edu},
issn={00062960},
coden={BICHA},
pubmed_id={17323919},
language={English},
abbrev_source_title={Biochemistry},
document_type={Article},
source={Scopus},
}

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Kinetics; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Denaturation; Sequence Alignment; Substrate Specificity; Thermotoga maritima, Thermotoga maritima","chemicals_cas":"4 nitrophenylgalactoside, 3150-24-1; alpha galactosidase, 9023-01-2; aspartic acid, 56-84-8, 6899-03-2; azide, 12596-60-0, 14343-69-2; glycine, 56-40-6, 6000-43-7, 6000-44-8; glycosidase, 9032-92-2; Azides; alpha-Galactosidase, 3.2.1.22","correspondence_address1":"Kelly, R.M.; Department of Chemical and Biomolecular Engineering, , Raleigh, NC 27695-7905, United States; email: rmkelly@eos.ncsu.edu","issn":"00062960","coden":"BICHA","pubmed_id":"17323919","language":"English","abbrev_source_title":"Biochemistry","document_type":"Article","source":"Scopus","bibtex":"@ARTICLE{Comfort20073319,\nauthor={Comfort, D.A. and Bobrov, K.S. and Ivanen, D.R. and Shabalin, K.A. and Harris, J.M. and Kulminskaya, A.A. and Brumer, H. and Kelly, R.M.},\ntitle={Biochemical analysis of Thermotoga maritima GH36 α-galactosidase (TmGalA) confirms the mechanistic commonality of clan GH-D glycoside hydrolases},\njournal={Biochemistry},\nyear={2007},\nvolume={46},\nnumber={11},\npages={3319-3330},\ndoi={10.1021/bi061521n},\nnote={cited By 72},\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-33947433621&doi=10.1021%2fbi061521n&partnerID=40&md5=0052f204a32353c216bae321a8599fe1},\naffiliation={Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, NC 27695-7905, United States; 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Kinetics; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Denaturation; Sequence Alignment; Substrate Specificity; Thermotoga maritima, Thermotoga maritima},\nchemicals_cas={4 nitrophenylgalactoside, 3150-24-1; alpha galactosidase, 9023-01-2; aspartic acid, 56-84-8, 6899-03-2; azide, 12596-60-0, 14343-69-2; glycine, 56-40-6, 6000-43-7, 6000-44-8; glycosidase, 9032-92-2; Azides; alpha-Galactosidase, 3.2.1.22},\ncorrespondence_address1={Kelly, R.M.; Department of Chemical and Biomolecular Engineering, , Raleigh, NC 27695-7905, United States; email: rmkelly@eos.ncsu.edu},\nissn={00062960},\ncoden={BICHA},\npubmed_id={17323919},\nlanguage={English},\nabbrev_source_title={Biochemistry},\ndocument_type={Article},\nsource={Scopus},\n}\n\n","author_short":["Comfort, D.","Bobrov, K.","Ivanen, D.","Shabalin, K.","Harris, J.","Kulminskaya, A.","Brumer, H.","Kelly, R."],"key":"Comfort20073319","id":"Comfort20073319","bibbaseid":"comfort-bobrov-ivanen-shabalin-harris-kulminskaya-brumer-kelly-biochemicalanalysisofthermotogamaritimagh36galactosidasetmgalaconfirmsthemechanisticcommonalityofclanghdglycosidehydrolases-2007","role":"author","urls":{"Paper":"https://www.scopus.com/inward/record.uri?eid=2-s2.0-33947433621&doi=10.1021%2fbi061521n&partnerID=40&md5=0052f204a32353c216bae321a8599fe1"},"keyword":["Anomeric stereochemistry; 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