Exam 9: Catalytic Strategies

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What type of reaction is catalyzed by proteases?

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Which of the following is an enzyme that temporarily undergoes covalent catalysis as part of its mechanism?

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What type of assay allows analysis of an enzyme catalyzed reaction in milliseconds?

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Binding of a water molecule to the zinc ion induces

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Describe the secondary and tertiary structures in domains that form P-loops and bind phosphoryl groups.

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The metal ion most commonly found at the active site of metalloproteases is

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What is the common nucleophile found in cysteine, metallo-, and aspartyl proteases?

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What do trypsin, subtilisin, and elastase have in common?

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A-T base pairs, which contain _____ hydrogen bonds, are more easily interrupted than G-C base pairs with _______ hydrogen bonds.

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What is significant about the slow rate for myosin's hydrolysis of ATP?

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EcoRV cleaves cognate DNA with a specificity approximately _____ times that of non-cognate DNA.

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In chymotrypsin, the tetrahedral intermediate transition state is stabilized by a structural feature referred to as the "___________________" hole.

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What metal ion is frequently found in enzyme active sites that act on phosphate-containing substrates?

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What features of carbonic anhydrase allow the rapid hydration of carbon dioxide?

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What type of symmetry is created by inverted repeats in double-stranded DNA?

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In proteases such as papain, a ___________________ residue is activated by hydrogen-bonding to a histidine residue.

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What is the common strategy for cysteine, metallo-, and aspartyl proteases?

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In trypsin, the specificity pocket contains a/an ______________ residue that binds to the positive charge of the K or R residue of the substrate.

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What supports the theory that a catalytic triad strategy is a result of convergent evolution?

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Which of the following is NOT a way in which enzymes stabilize a transition state?

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