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Author Zuccotti, Simone ♦ Rosano, Camillo ♦ Bemporad, Francesco ♦ Stefani, Massimo ♦ Bolognesi, Martino
Source World Health Organization (WHO)-Global Index Medicus
Content type Text
Publisher Wiley
File Format HTM / HTML
Language English
Difficulty Level Medium
Subject Domain (in DDC) Computer science, information & general works ♦ Library & information sciences ♦ Natural sciences & mathematics ♦ Chemistry & allied sciences ♦ Crystallography ♦ Life sciences; biology ♦ Physiology & related subjects ♦ Biochemistry ♦ Natural history of organisms ♦ Technology ♦ Medicine & health ♦ Human physiology ♦ Pharmacology and therapeutics ♦ Diseases ♦ Manufacture for specific uses ♦ Precision instruments & other devices
Subject Domain (in MeSH) Archaea ♦ Organisms ♦ Enzymes and Coenzymes ♦ Amino Acids, Peptides, and Proteins ♦ Chemicals and Drugs ♦ Investigative Techniques ♦ Analytical, Diagnostic and Therapeutic Techniques and Equipment ♦ Physical Phenomena ♦ Chemical Phenomena ♦ Biological Sciences ♦ Information Science ♦ Information Science
Subject Keyword Discipline Crystallography ♦ Discipline Biophysics ♦ Discipline Molecular Biology ♦ Discipline Biochemistry ♦ Acid Anhydride Hydrolases ♦ Chemistry ♦ Sulfolobus Solfataricus ♦ Enzymology ♦ Isolation & Purification ♦ Metabolism ♦ Amino Acid Sequence ♦ Archaeal Proteins ♦ Crystallization ♦ Molecular Sequence Data ♦ Protein Denaturation ♦ Protein Folding ♦ Thermodynamics ♦ X-ray Diffraction ♦ Journal Article ♦ Research Support, Non-u.s. Gov't
Abstract Acylphosphatase is a ubiquitous small enzyme that was first characterized in mammals. It is involved in the hydrolysis of carboxyl-phosphate bonds in several acylphosphate substrates, such as carbamoylphosphate and 1,3-biphosphoglycerate; however, a consensus on acylphosphatase action in vivo has not yet been reached. Recent investigations have focused on acylphosphatases from lower phyla, such as Drosophila melanogaster and Escherichia coli, in view of the application of these small proteins as models in the study of folding, misfolding and aggregation processes. An acylphosphatase from the hyperthermophilic archaeon Sulfolobus solfataricus has been cloned, expressed and purified. Here, the growth and characterization of a triclinic and a monoclinic crystal form of the hyperthermophilic enzyme are reported; X-ray diffraction data have been collected to 1.27 and 1.90 A resolution, respectively.
Description Country affiliation: Italy
Author Affiliation: Zuccotti S ( Department of Physics-INFM, Center of Excellence for Biomedical Research, University of Genova, Via Dodecaneso 33, 16132 Genova, Italy.)
ISSN 2053230X
Educational Role Student ♦ Teacher
Age Range above 22 year
Educational Use Reading ♦ Research ♦ Self Learning
Interactivity Type Expositive
Education Level UG and PG
Learning Resource Type Article
Publisher Date 2005-01-01
Publisher Place Great Britain (UK)
e-ISSN 17443091
Journal Acta Crystallographica Section F Structural Biology and Crystallization Communications
Volume Number 61
Issue Number Pt 1


Source: WHO-Global Index Medicus