PPT-Enzyme Catalytic Mechanisms II

Dr Kevin Ahern Protease Mechanisms Aspartic Acid Aspartic Acid Histidine Cysteine Electron rich Metal Other Protease Families Cysteine Aspartyl Metallo Papain Cathepsin D Carboxypeptidase A. Inhibition is a term used to describe the inability of a product being formed due to the presence of another substance (the inhibitor). Enzyme inhibition . can be competitive or noncompetitive. Competitive inhibition is caused when an inhibitor “competes” with the substrate in binding with the enzyme. Pratt & . Cornely. . Ch. 7. Other Factors. Other factors affect enzyme activity. Temperature. pH . pH Optimum. Determined by structural stability. Compartmentalization. Determined by active site residues. Mechanisms. C483 Spring 2013. Questions. 1. . Replacement of the amino acid ________ at or near an active site of an enzyme is more likely to change enzyme activity than the replacement of ________ at or near the active site.. Transferases and hydrolases catalyze group transfer reactions. Acyl transfer:. Hexo. kinase. catalyzes a phosphoryl transfer from ATP to glucose. Glycosidases. are hydrolases, catalyzing hydrolysis of . (CRE) is the field that studies the rates and mechanisms of chemical reactions and the design of the reactors in which they take place.. Lecture 18. Web Lecture 18. Class Lecture . 23–Tuesday 4/16/2013. Transferases and hydrolases catalyze group transfer reactions. Acyl transfer:. Hexo. kinase. catalyzes a phosphoryl transfer from ATP to glucose. Glycosidases. are hydrolases, catalyzing hydrolysis of . (CRE) is the field that studies the rates and mechanisms of chemical reactions and the design of the reactors in which they take place.. Lecture 18. Web Lecture 18. Class . Lecture . 23–Tuesday. Catalytic Mechanisms . Katja. Dove. PhD Candidate, . Department of Biochemistry, University of Washington. Email: Katja.Dove@seattlecolleges.edu. Please turn in your take-home part for midterm 1 BEFORE class. I will hand back in-class exams at the end of class today. 27. th. September 2017. www.uniprot.org. The two sides of UniProtKB. curated by experts. data from scientific papers. annotation of sequence features. collates isoforms in one entry. annotation from rule systems (incl. expert-curated rules). Theories of Enzyme Evolution. Overview. (1) . Divergent. . retrograde. evolution, recruiting . adjacent enzymes in pathway. and constrained by . binding similar molecules . as substrates or products.. . biological . catalysts. . . . proteinaceous. . . specific . catalytic site . (active . centre. ). . some enzymes contain . . “. cofactor. ”( nonprotein organic compound) . . catalytically active. Posttranscriptional Control Mechanisms. mRNAs Are Degraded at Different Rates. The range of mRNA stability in eukaryotic cells, measured in half-lives, varies from a few minutes to many hours or days. The mRNA molecules themselves appear to contain elements that dictate their decay rates. These elements include the poly(A) tail, the 5′ cap, and sequences that are located within the coding region. A major route for mRNA degradation begins with the progressive removal of its poly(A) tail, a process catalyzed by . E. . Vesselli. Physics Dept. and CENMAT, . Università. . degli. . Studi. di . Trieste (Italy. ). and. Laboratorio. . TASC IOM-CNR (Italy. ). . vesselli@iom.cnr.it. About the importance of. CO and CO2 catalytic reduction. th. , 4:00 PM. HUTCHISON HALL 473. UNIVERSITY OF ROCHESTER, DEPARTMENT OF CHEMISTRY. ORGANIC SEMINAR. Friday, January 15. th. , 2016. 9:00 a.. University of Rochester. “Catalytic Transformations that Utilize Bimetallic Cooperation”.