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Protein engineering of bacterial alpha-amylases.
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Europe PubMed Central
PubMed ID
11150610
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11150610%20AND%20SRC:MED&resulttype=core&format=json
retrieved
3 November 2019
review article
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Europe PubMed Central
title
Protein engineering of bacterial alpha-amylases
(English)
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Europe PubMed Central
PubMed ID
11150610
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11150610%20AND%20SRC:MED&resulttype=core&format=json
retrieved
3 November 2019
author
Jens Erik Nielsen
series ordinal
1
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Europe PubMed Central
PubMed ID
11150610
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11150610%20AND%20SRC:MED&resulttype=core&format=json
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3 November 2019
author name string
T V Borchert
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2
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Europe PubMed Central
PubMed ID
11150610
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11150610%20AND%20SRC:MED&resulttype=core&format=json
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3 November 2019
language of work or name
English
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publication date
1 December 2000
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Europe PubMed Central
PubMed ID
11150610
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3 November 2019
published in
Biochimica et Biophysica Acta
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Europe PubMed Central
PubMed ID
11150610
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11150610%20AND%20SRC:MED&resulttype=core&format=json
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3 November 2019
volume
1543
1 reference
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Europe PubMed Central
PubMed ID
11150610
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11150610%20AND%20SRC:MED&resulttype=core&format=json
retrieved
3 November 2019
page(s)
253-274
1 reference
stated in
Europe PubMed Central
PubMed ID
11150610
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11150610%20AND%20SRC:MED&resulttype=core&format=json
retrieved
3 November 2019
issue
2
1 reference
stated in
Europe PubMed Central
PubMed ID
11150610
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11150610%20AND%20SRC:MED&resulttype=core&format=json
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3 November 2019
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Site-directed mutations in tyrosine 195 of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 affect activity and product specificity
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Crystal structure of calcium-depleted Bacillus licheniformis alpha-amylase at 2.2 A resolution
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Protein engineering in the alpha-amylase family: catalytic mechanism, substrate specificity, and stability
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Catalytic center of cyclodextrin glycosyltransferase derived from X-ray structure analysis combined with site-directed mutagenesis
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X-ray structure of cyclodextrin glycosyltransferase complexed with acarbose. Implications for the catalytic mechanism of glycosidases
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Crystallographic studies of the interaction of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 with natural substrates and products
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New conserved amino acid region of alpha-amylases in the third loop of their (beta/alpha)8-barrel domains
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Invariant glycines and prolines flanking in loops the strand beta 2 of various (alpha/beta)8-barrel enzymes: a hidden homology?
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based on heuristic
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Characteristic differences in the primary structure allow discrimination of cyclodextrin glucanotransferases from alpha-amylases
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Crossref
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Catalytic mechanism of enzymic glycosyl transfer
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Mechanisms of enzymatic glycoside hydrolysis
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7 January 2021
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Structures and mechanisms of glycosyl hydrolases
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based on heuristic
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X-ray structures along the reaction pathway of cyclodextrin glycosyltransferase elucidate catalysis in the alpha-amylase family
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Crossref
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Functional relationships between cyclodextrin glucanotransferase from an alkalophilic Bacillus and alpha-amylases. Site-directed mutagenesis of the conserved two Asp and one Glu residues
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Site-directed mutagenesis of active site residues in Bacillus subtilis alpha-amylase
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based on heuristic
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The concept of the alpha-amylase family: structural similarity and common catalytic mechanism
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Model for inactivation of alpha-amylase in the presence of salts: theoretical and experimental studies.
1 reference
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based on heuristic
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Kinetic study of the irreversible thermal denaturation of Bacillus licheniformis alpha-amylase
1 reference
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7 January 2021
based on heuristic
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Investigation of the mechanisms of irreversible thermoinactivation of Bacillus stearothermophilus alpha-amylase
1 reference
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Crossref
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7 January 2021
based on heuristic
inferred from DOI database lookup
Improved thermostability of a Bacillus alpha-amylase by deletion of an arginine-glycine residue is caused by enhanced calcium binding.
1 reference
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7 January 2021
based on heuristic
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Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding
1 reference
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7 January 2021
based on heuristic
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Thermostabilization by Proline Substitution in an Alkaline, Liquefying α-Amylase from Bacillus sp. Strain KSM-1378
1 reference
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Hyperthermostable variants of a highly thermostable alpha-amylase
1 reference
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7 January 2021
based on heuristic
inferred from DOI database lookup
Hyperthermostable mutants of Bacillus licheniformis alpha-amylase: multiple amino acid replacements and molecular modelling.
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900240-5
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7 January 2021
based on heuristic
inferred from DOI database lookup
Protein engineering of alpha-amylase for low pH performance
1 reference
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Crossref
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7 January 2021
based on heuristic
inferred from DOI database lookup
On the pH dependence of protein stability.
1 reference
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7 January 2021
based on heuristic
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The active center of a mammalian alpha-amylase. Structure of the complex of a pancreatic alpha-amylase with a carbohydrate inhibitor refined to 2.2-A resolution
1 reference
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7 January 2021
based on heuristic
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The pKa of the general acid/base carboxyl group of a glycosidase cycles during catalysis: a 13C-NMR study of bacillus circulans xylanase
1 reference
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based on heuristic
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Contribution of long-range electrostatic interactions to the stabilization of the catalytic transition state of the serine protease subtilisin BPN'
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7 January 2021
based on heuristic
inferred from DOI database lookup
Electrostatics in the active site of an alpha-amylase
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7 January 2021
based on heuristic
inferred from DOI database lookup
Protein engineering of Aspergillus awamori glucoamylase to increase its pH optimum.
1 reference
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7 January 2021
based on heuristic
inferred from DOI database lookup
Cassette mutagenesis of Aspergillus awamori glucoamylase near its general acid residue to probe its catalytic and pH properties
1 reference
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based on heuristic
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Nanometric design of extraordinary hydrophobic-induced pKa shifts for aspartic acid: relevance to protein mechanisms
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7 January 2021
based on heuristic
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Identifiers
DOI
10.1016/S0167-4838(00)00240-5
1 reference
stated in
Europe PubMed Central
PubMed ID
11150610
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11150610%20AND%20SRC:MED&resulttype=core&format=json
retrieved
3 November 2019
PubMed ID
11150610
1 reference
stated in
Europe PubMed Central
PubMed ID
11150610
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11150610%20AND%20SRC:MED&resulttype=core&format=json
retrieved
3 November 2019
ResearchGate publication ID
12178086
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