Course: Enzymology

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Course title Enzymology
Course code KBBV/C672
Organizational form of instruction Lecture
Level of course Master
Year of study not specified
Semester Summer
Number of ECTS credits 4
Language of instruction Czech
Status of course Compulsory-optional
Form of instruction Face-to-face
Work placements This is not an internship
Recommended optional programme components None
Lecturer(s)
  • Štěpánková Šárka, Mgr. Ph.D.
  • Čegan Alexander, prof. Ing. CSc.
Course content
History of enzymology; subconscious using of enzymes. Structure of enzymes (holoenzyme, apoenzyme, cofactor). Multiple forms of enzymes (isoenzymes, polymeric enzymes), multienzymes (multienzyme complexes, polypeptides). Enzyme nomenclature (trivial, semisystematic, systematic). Classification of enzymes. Enzyme activity (catalytic, specific). Conventional activity units. methods for determination of enzyme activity (optical, electrochemical). Mechanism of enzyme catalysis (thermodynamics and kinetics of conversion of substrate to product). Formation of complex enzyme-substrate. Energetic profile of noncatalysed and catalysed reaction, possibilities to affect of activation ebergy. Enzyme kinetics. Influence of reaction conditions (t, pH, ionic strenght) and effectors on velocity of enzymatic reaction. Kinetics of enzymatic reaction in steady state. Kinetics of uni-substrate reactions (Michaelis-Menten equation). Kinetics of multi-substrate reactions. Software for enzyme konetics. Inhibition of enzymes. Inhibition by substrate, product, inhibitor. Reversible/irreversible inhibitors. Types of full inhibition (competitive, noncompetitive, uncompetitive, mixed). Cooperativity in enzyme action. Homotropic and heterotropic, cooperativity, allosteric effect. Isolation of enzymes. Animal, plant, microbial sources of enzymes. Releasing of intracellular enzymes from cells. Choice of separative techniques. Purification procedures. Study of enzyme structure. Crystallization of enzymes. X-ray crystallography. Enzymes in biochemical analytics. Determination of clinical important enzymes. Determination of analytes using solute enzymes. Immobilization of enzymes. Applications. Enzyme biosensors. Enzyme immunoanalysis. Enzymatic markers and methods of preparation of enzyme conjugates. The most important practically used enzymes. Examples of use (medicine, food processing, laundry, organic synthesis).

Learning activities and teaching methods
Monologic (reading, lecture, briefing)
Learning outcomes
The aim of this subject is to intensify knowledge of enzymology gained in subject General Biochemistry and Clinical Biochemistry.
Students will get basic information about properties of enzymes, their structure, partition, nomenclature, mechanism of catalytic action, enzyme kinetics and practical applications of enzymes.
Prerequisites
unspecified

Assessment methods and criteria
Oral examination, Written examination

not specified
Recommended literature
  • Bisswanger H. Practical Enzymology, Wiley, John & Sons, Incorporated, 2004. ISBN 3527304444.
  • Cohnheim O. Enzymes, BiblioBazaar, 2009. ISBN 1113706155.
  • Kolev D. Enzymology. World Scientific Pub Co Inc, 2008. ISBN 9810227965.
  • Vodrážka Z., Rauch P., Káš J. Enzymologie, VŠCHT, 1998. ISBN 8070803304.


Study plans that include the course
Faculty Study plan (Version) Category of Branch/Specialization Recommended year of study Recommended semester
Faculty: Faculty of Chemical Technology Study plan (Version): Bioanalyst (2016) Category: Chemistry courses 1 Recommended year of study:1, Recommended semester: Summer
Faculty: Faculty of Chemical Technology Study plan (Version): Bioanalyst (2015) Category: Chemistry courses 1 Recommended year of study:1, Recommended semester: Summer
Faculty: Faculty of Chemical Technology Study plan (Version): Bioanalyst (2013) Category: Chemistry courses 1 Recommended year of study:1, Recommended semester: Summer