Unit BIOORGANIC CHEMISTRY
- Course
- Pharmaceutical biotechnologies
- Study-unit Code
- GP003555
- Location
- PERUGIA
- Curriculum
- In all curricula
- Teacher
- Francesca Marini
- Teachers
-
- Francesca Marini
- Hours
- 42 ore - Francesca Marini
- CFU
- 6
- Course Regulation
- Coorte 2022
- Offered
- 2022/23
- Learning activities
- Caratterizzante
- Area
- Discipline di base applicate alle biotecnologie
- Academic discipline
- CHIM/06
- Type of study-unit
- Obbligatorio (Required)
- Type of learning activities
- Attività formativa monodisciplinare
- Language of instruction
- Italian
- Contents
- Bioorganic chemistry applies the principles of organic chemistry on interdisciplinary topics related to biochemistry, pharmaceutical chemistry and biotechnology. The main purpose of this course is to provide knowledge on the catalytic mechanisms of enzymes and their applications in bioconversions from an organic chemistry perspective. In the first part of the course, the similarities between organic reactions and biochemical transformations are highlighted and the catalytic mechanisms of certain classes of enzymes and the role of some coenzymes discussed. In the second part, an introduction to the use of enzymes in organic synthesis (biocatalysis) and the production of some enantiopure molecules is provided.
- Reference texts
- Lecture slides complemented by assigned additional readings.
For further readings:
J. E. McMurry, T.Begley The Organic Chemistry of Biological Pathways, Roberts & Co. 2005P.
Y. BRUICE, Organic Chemistry, Pearson. T.D. Bugg "Introduction to Enzyme and Coenzyme Chemistry"3° Edition John Wiley & Sons, Ltd, 2012.
K.Faber Biotransformations in Organic Chemistry, Springer-Verlag, 2011. - Educational objectives
- At the end of the course students understand how the principles of mechanistic organic chemistry can be applied to the study of biological pathways, drug design and biocatalysis. Students will acquire knowledge on catalytic mechanisms of certain classes of enzymes and different aspects of biocatalysis. They are able to discuss chemical aspects of biological transformations and apply the acquired knowledge to the discussion of examples from scientific literature.
- Prerequisites
- In order to understand the course contents and achieve the learning outcomes students should have basic knowledge of Organic Chemistry.
- Teaching methods
- Lectures covering all the subjects of the course.
- Other information
- The attendance is strongly recommended.
- Learning verification modality
- The oral exam (approximately 30 minutes) is addressed to verify the understanding and the ability to clearly communicate the topics covered in the course. The ability to apply acquired knowledge to the discussion of enzymatic mechanisms and biocatalytic transformations, also selected from literature, will be evaluated. For information about support services for students with disabilities and / or DSA visit the page http://www.unipg.it/disabilita-e-dsa
- Extended program
- Introduction to bioorganic chemistry. Acidity and pKa in bioorganic chemistry. Stereochemistry and chirality. Stereogenic and prostereogenic units. Similarities between organic reactions and biochemical transformations. Common Organic Mechanisms in Biological Chemistry. Biosynthesis of terpenes and polyketides. Chemical catalysis and enzymatic catalysis: general principles. Acid catalysis and base catalysis, nucleophilic catalysis, metal catalysis. Effects of proximity, orientation and distortion. Catalytic perfection. Examples of catalytic mechanisms of some classes of enzymes: protein kinases, serinproteases, cystein proteases, aspartate proteases, metal proteases and glycosidases. Aldolases. Enzymes as drug target. Coenzymes. NAD and FAD in redox processes. Roles in catalytic mechanisms of biotin, K vitamin, thiamine pyrophosphate, S-adenosylmethionine and pyridoxal phosphate. Introduction to biocatalysis: use of microrganism and isolated enzymes in the production of organic molecules. Enzymes in organic solvents. Immobilized enzymes and modified enzymes for performance optimization. Enzymatic kinetic resolutions. Dynamic kinetic resolutions. Methods for the measurement of the enantiomeric excess. Examples of application of hydrolytic enzymes in the production of enantiopure amino acids and intermediates of pharmaceutical interest. Asymmetric synthesis from optically inactive substrates. Use of dehydrogenases in biocatalysis and recycling of the cofactor. Catalytic Antibodies.
The course contains topics related to sustainability (biocatalysis)