ENZYME
... a propeptide (19-133) and the mature peptide (134-345). The amino acid numbers are based on the mature peptide. The protein is stabilised by three disulfide bridges. ...
... a propeptide (19-133) and the mature peptide (134-345). The amino acid numbers are based on the mature peptide. The protein is stabilised by three disulfide bridges. ...
Amino Acid Synthesis
... – Glutamine synthetase incorporates amino group • Glutamine serves as nitrogen donor for nucleic acids, etc. ...
... – Glutamine synthetase incorporates amino group • Glutamine serves as nitrogen donor for nucleic acids, etc. ...
Section 6 – Catalysis
... Some enzymes are activated by phosphorylation, others are inactivated (and vice versa for dephosphorylation) ...
... Some enzymes are activated by phosphorylation, others are inactivated (and vice versa for dephosphorylation) ...
Document
... Prosthetic group – non amino acid portion of the enzyme needed for catalysis. Often a coenzyme or metal ion. Holoenzyme – complete catalytically active enzyme, with all ...
... Prosthetic group – non amino acid portion of the enzyme needed for catalysis. Often a coenzyme or metal ion. Holoenzyme – complete catalytically active enzyme, with all ...
Chapter 8
... backbone • Tertiary – interactions between R groups • Quaternary – more than 1 polypeptide subunit ...
... backbone • Tertiary – interactions between R groups • Quaternary – more than 1 polypeptide subunit ...
ENZYMES (Basic Concepts and Kinetics) (Chapter 8)
... The Effects of Enzyme Inhibitors 1. Competitive In the presence of a competitive inhibitor, it takes a higher substrate concentration to achieve the same velocities that were reached in its absence. So while Vmax can still be reached if sufficient substrate is available, one-half Vmax requires a h ...
... The Effects of Enzyme Inhibitors 1. Competitive In the presence of a competitive inhibitor, it takes a higher substrate concentration to achieve the same velocities that were reached in its absence. So while Vmax can still be reached if sufficient substrate is available, one-half Vmax requires a h ...
lec1-introduction
... one of the 6 major classes of enzyme activity the subclass (type of substrate or bond cleaved) the sub-subclass (group acted upon, cofactor required, etc...) a serial number… (order in which enzyme was added to list) ...
... one of the 6 major classes of enzyme activity the subclass (type of substrate or bond cleaved) the sub-subclass (group acted upon, cofactor required, etc...) a serial number… (order in which enzyme was added to list) ...
New vistas in anti-retroviral HIV drug design
... positions of mobile hydrogen atoms and protons. Neutron crystallography, however, can reveal these hydrogen-bonding interactions, which play a key role in how effectively a drug binds to its target. Researchers used neutron crystallography to probe the structure of HIV-1 protease in complex with the ...
... positions of mobile hydrogen atoms and protons. Neutron crystallography, however, can reveal these hydrogen-bonding interactions, which play a key role in how effectively a drug binds to its target. Researchers used neutron crystallography to probe the structure of HIV-1 protease in complex with the ...
Unit 2 Test Review
... Organic compound that is the building block of organisms; made of amino acids Number (from 0-14) measuring the amount of hydrogen ions in a solution Molecules made during chemical reactions; on the right side of the equation A chemical that releases hydrogen ions in a solution Chemicals centered aro ...
... Organic compound that is the building block of organisms; made of amino acids Number (from 0-14) measuring the amount of hydrogen ions in a solution Molecules made during chemical reactions; on the right side of the equation A chemical that releases hydrogen ions in a solution Chemicals centered aro ...
Catalytic triad
A catalytic triad refers to the three amino acid residues that function together at the centre of the active site of some hydrolase and transferase enzymes (e.g. proteases, amidases, esterases, acylases, lipases and β-lactamases). An Acid-Base-Nucleophile triad is a common motif for generating a nucleophilic residue for covalent catalysis. The residues form a charge-relay network to polarise and activate the nucleophile, which attacks the substrate, forming a covalent intermediate which is then hydrolysed to regenerate free enzyme. The nucleophile is most commonly a serine or cysteine amino acid, but occasionally threonine. Because enzymes fold into complex three-dimensional structures, the residues of a catalytic triad can be far from each other along the amino-acid sequence (primary structure), however, they are brought close together in the final fold.As well as divergent evolution of function (and even the triad's nucleophile), catalytic triads show some of the best examples of convergent evolution. Chemical constraints on catalysis have led to the same catalytic solution independently evolving in at least 23 separate superfamilies. Their mechanism of action is consequently one of the best studied in biochemistry.