Computer-aided analysis of spatial structure of some hydrolytic enzymes

Using the MolScript version 2.1 computer program for protein molecule modeling and X-ray structure analysis data the spatial structures of several hydrolytic enzymes have been compared. These include glucoamylase from Aspergillus awamori and Saccharomycopsis fibuligera and lipases from Rhizopus japo...

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Bibliographic Details
Published in:Biochemistry (Moscow) 2005-10, Vol.70 (10), p.1086-1094
Main Authors: Artyukhov, V G, Kovaleva, T A, Kozhokina, O M, Bitutskaya, L A, Dronov, R V, Trofimova, O D
Format: Article
Language:English
Subjects:
Algebraic topology
Amino Acid Sequence
Amino acids
Aspergillus - enzymology
Aspergillus awamori
Binding Sites
Computer Simulation
Crystallography, X-Ray
Enzymes
Glucan 1,4-alpha-Glucosidase - chemistry
Glucan 1,4-alpha-Glucosidase - metabolism
Glycoside Hydrolases - chemistry
Glycoside Hydrolases - metabolism
Hydrogen-Ion Concentration
Lipase - chemistry
Lipase - metabolism
Molecular Sequence Data
Protein Conformation
Rhizopus
Rhizopus - enzymology
Saccharomycopsis - enzymology
Saccharomycopsis fibuligera
Substrate Specificity
Topology
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Summary:Using the MolScript version 2.1 computer program for protein molecule modeling and X-ray structure analysis data the spatial structures of several hydrolytic enzymes have been compared. These include glucoamylase from Aspergillus awamori and Saccharomycopsis fibuligera and lipases from Rhizopus japonicus. Results on homology of amino acid sequences and topology of secondary structure elements were obtained. 3D models of these enzymes with positioning of functionally important groups in the active site cavity were built.
ISSN:0006-2979
1608-3040
0320-9725
DOI:10.1007/s10541-005-0229-6