(Q33183952)

English

Iterative database searches demonstrate that glycoside hydrolase families 27, 31, 36 and 66 share a common evolutionary origin with family 13.

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scholarly article

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Europe PubMed Central

PubMed publication ID

23 July 2017

Iterative database searches demonstrate that glycoside hydrolase families 27, 31, 36 and 66 share a common evolutionary origin with family 13. (English)

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Europe PubMed Central

PubMed publication ID

23 July 2017

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Daniel J. Rigden

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Daniel J Rigden

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Europe PubMed Central

PubMed publication ID

23 July 2017

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publication date

1 July 2002

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Europe PubMed Central

PubMed publication ID

23 July 2017

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Europe PubMed Central

PubMed publication ID

23 July 2017

523

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Europe PubMed Central

PubMed publication ID

23 July 2017

1-3

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Europe PubMed Central

PubMed publication ID

23 July 2017

17-22

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Europe PubMed Central

PubMed publication ID

23 July 2017

A classification of glycosyl hydrolases based on amino acid sequence similarities

1 reference

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New families in the classification of glycosyl hydrolases based on amino acid sequence similarities

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The ENZYME database in 2000

1 reference

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Structures and mechanisms of glycosyl hydrolases

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Glycoside hydrolases and glycosyltransferases: families and functional modules

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Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases

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beta-fructosidase superfamily: homology with some alpha-L-arabinases and beta-D-xylosidases

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Prediction of a common beta-propeller catalytic domain for fructosyltransferases of different origin and substrate specificity

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Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes

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T-Coffee: A novel method for fast and accurate multiple sequence alignment

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CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

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The Pfam protein families database

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Protein secondary structure prediction based on position-specific scoring matrices

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Comparison of sequence profiles. Strategies for structural predictions using sequence information

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Enhanced genome annotation using structural profiles in the program 3D-PSSM

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LiveBench-2: large-scale automated evaluation of protein structure prediction servers.

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CDD: a database of conserved domain alignments with links to domain three-dimensional structure

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Comparative protein modelling by satisfaction of spatial restraints

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How far divergent evolution goes in proteins

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Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database searches

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Unequivocal identification of Asp-214 as the catalytic nucleophile of Saccharomyces cerevisiae alpha-glucosidase using 5-fluoro glycosyl fluorides

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Carboxyl group of residue Asp647 as possible proton donor in catalytic reaction of alpha-glucosidase from Schizosaccharomyces pombe

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Crystal structure of a maltogenic amylase provides insights into a catalytic versatility

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The structure of human pancreatic alpha-amylase at 1.8 A resolution and comparisons with related enzymes

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The TIM-barrel fold: a versatile framework for efficient enzymes

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The (betaalpha)(8) glycosidases: sequence and structure analyses suggest distant evolutionary relationships.

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A group of alpha-1,4-glucan lyases and their genes from the red alga Gracilariopsis lemaneiformis: purification, cloning, and heterologous expression

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Beta-glucosidase, beta-galactosidase, family A cellulases, family F xylanases and two barley glycanases form a superfamily of enzymes with 8-fold beta/alpha architecture and with two conserved glutamates near the carboxy-terminal ends of beta-strand

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ALSCRIPT: a tool to format multiple sequence alignments

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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

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Conserved sequence motifs in levansucrases and bifunctional beta-xylosidases and alpha-L-arabinases

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Structure prediction meta server

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Barrels in pieces?

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Identifiers

10.1016/S0014-5793(02)02879-X

1 reference

Europe PubMed Central

PubMed publication ID

23 July 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

23 July 2017

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