Notes in g. Enzyme Kinetics

To Subscribe, use this Key


Status Last Update Fields
Published 07/28/2024 The steady state assumption assumes?
Published 07/28/2024 The Michaelis-Menten equation states:
Published 07/28/2024 A {{c1::competitive}} inhibitor binds at the same site as the substrate and competes with the substrate for binding to the active site
Published 07/28/2024 A {{c1::noncompetitive}} inhibitor binds to a site other than the active site but prevents the enzyme from adopting a conformation that is requir…
Published 07/28/2024 a609ed1f88b640b4a006e1b154388c8f-ao-1
Published 07/28/2024 a609ed1f88b640b4a006e1b154388c8f-ao-2
Published 07/28/2024 a609ed1f88b640b4a006e1b154388c8f-ao-3
Published 07/28/2024 a609ed1f88b640b4a006e1b154388c8f-ao-4
Published 07/28/2024 {{c1::Suicide}} inhibition uses substrate mimics that irreversibly modify an enzyme's active site
Published 07/28/2024 dTMP is formed from dUMP through the action of the enzyme {{c1::thymidilate synthase}}
Published 07/28/2024 Thymidilate synthase uses the cofactor {{c1::N5,N10-Methylene-THF}} to methylate dUMP, forming dTMP
Published 07/28/2024 During the activity of thymidilate synthase, {{c1::N5,N10-methylene-THF}} is the methyl donor in dTMP synthesis
Published 07/28/2024 {{c1::FdUMP}} is a {{c2::suicide}} inhibitor used to terminate {{c3::thymidilate synthase}} methylation of dUMP to dTMP
Published 07/28/2024 {{c1::Dihydrofolate reductase}} is the enzyme responsible for converting dihydrofolate to tetrahydrofolate 
Published 07/28/2024 What 3 factors contributes to the reactivity of Serine proteases?
Published 07/28/2024 HIV synthesisizes its proteins as {{c1::polyproteins}}
Published 07/28/2024 The active sites of both monomers of the HIV protease dimer contain {{c1::aspartate}} residues. 
Published 07/28/2024 {{c1::Indinavir}} is a {{c2::peptidomimetic competitive inhibitor}} used in the treatment of {{c2::HIV}} and is an example of structure aided des…
Published 07/28/2024 {{c1::Zymogens}} are the inactive precursors of enzymes
Published 07/28/2024 Chymotrypsinogen is activated by {{c1::trypsin}}
Published 07/28/2024 Trypsinogen is activated by {{c1::enteropeptidase}}
Published 07/28/2024 Proelastase is activated by {{c1::trypsin}}
Published 07/28/2024 Procarboxypeptidase is activated by {{c1::trypsin}}
Published 07/28/2024 Prolipase is activated by {{c1::trypsin}}
Published 07/28/2024 Fibrinogen is activated by {{c1::thrombin}}
Published 07/28/2024 Thimidylate synthase uses {{c1::cysteine}} sidechain for catalysis
Published 07/28/2024 How does FdUMP inhibit dTMP biosynthesis?
Published 07/28/2024 What are two ways to inhibit dTMP biosynthesis?
Published 07/28/2024 Dihydrofolate reductase uses cofactor {{c1::NADPH}} to convert DHF into THF • {{c1::Methotrexate}} is a competitive inhibitor of DHFR • Anticancer age…
Published 07/28/2024 How can serine proteases be inhibited?
Published 07/28/2024 Oxyanion hole stabilizes {{c1::tetrahedral intermediate}} of serine proteases by {{c1::H bonding}} from {{c1::amide hydrogens}} of the enzym…
Published 07/28/2024 How are specifity pockets of chymotrypsin, trypsin and elastase organized?
Published 07/28/2024 HIV proteases cleaves at carboxy terminus of {{c1::hydrophobic}} amino acids
Published 07/28/2024 HIV protease is a {{c1::dimer::monomer/dimer}}. It contains 2 {{c1::ASP}} residues that catalyze through {{c1::General Acids/General Bases}} mech…
Published 07/28/2024 Activation of chymotripsinogen requires formation of ionic bond between {{c2::the N-terminus of Ile16}} and {{c1::Asp 194}} after cleavage
Published 07/28/2024 Three residues involved in polymerization of fibrin are {{c1::Gly-His-Arg}}
Published 07/28/2024 Two pathways involved in blood clotting are {{c1::intrinsic}} and {{c1::extrinsic}} pathways. Both involve {{c1::serine}} proteases
Published 07/28/2024 Penicillin inhibits {{c1::bacterial wall synthesis by suicide inhibition}} thereby preventing glycopeptide transpeptidase from forming the pentaglycin…
Status Last Update Fields