What three amino acids are found in the catalytic triad of chymotrypsin? Glu, Hi
ID: 495030 • Letter: W
Question
What three amino acids are found in the catalytic triad of chymotrypsin? Glu, His, Thr Ser, Arg, Cys Asp, His, Ser Cys, Lys, Glu Asn, His, Thr Of all the species that enzymes bind, they are thought to bind most tightly to. substrates products transition states intermediates all are bound very tightly In the chymotrypsin mechanism, what is used to stabilize the negative charge on the carbonyl oxygen of the transition state? hydrogen bonding between the enzyme and the anion from the carbonyl oxygen electrostatic interaction of the positively charged His and carbonyl oxygen electrostatic interaction of the negatively charged Asp and carbonyl oxygen electrostatic interaction of the active site Zn^2+ and carbonyl oxygen all of the above The ability for an enzyme to change its shape upon substrate binding represents the concept of lock and key induced fit proximity and orientation effects covalent catalysis none of the above The enzyme hexokinase catalyzes a reaction where its substrates are completely sequestered from the aqueous environment allowing for interactions to occur between enzyme and substrates that would not normally occur in an aqueous environment. What term describes this type of catalysis? electrostatic catalysis desolvation catalysis non-aqueous catalysiExplanation / Answer
Q 21
Answer C.
serine 195,
histidine 57,
and aspartate 102
Q 22
Of all thespecies that enzymes bind, they are thought to bind most tightly ...
Answer
C) transition states
Q 23
In the chymotrypsin mechanism, what is used to stabilize the negative charge on the carbonyl oxygen of the transition state
Answer
A) hydrogen bonding between the enzyme and the anion from the carbonyl oxygen
Q 24
The ability for an enzyme to change its shape upon substrate binding represents the concept of ___
Answer
b) induced fit
Q 25
The enzyme hexokinase catalyzes a reaction where its substrates are completely sequesteredfrom the aqueous environment allowing for interactions to occur between enzyme and substratesthat would not normally occur in an aqueous environment.
What term describes this type of catalysis?
Answer
A) electrostatic catalysis
catalytic triad : it is a set of three is a gathering of three amino acids that are found in the dynamic locales of a few proteases required in catalysis.
Three distinct proteases that have reactant groups of three are: chymotrypsin, trypsin and elastase. In chymotrypsin, the reactant set of three is produced using serine 195, histidine 57, and aspartate 102. The side chain of serine is clung to the imidazole ring of the histidine deposit which acknowledges a proton from serine to shape a solid alkoxide nucleophile within the sight of a substrate for assault. The aspartate deposit situates histidine to improve it a proton acceptor by means of hydrogen holding and electrostatic responses.
=========================================
induced fit model: it is a proposed instrument of collaboration between a protein and a substrate. It proposes that introduction of a compound to a substrate causes the dynamic site of the catalyst to change shape with a specific end goal to permit the protein and substrate to tie (see enzyme–substrate complex).
===================================================
Electrostatic catalysis
Adjustment of charged move states can likewise be by buildups in the dynamic site shaping ionic bonds (or halfway ionic charge associations) with the middle of the road. These bonds can either originate from acidic or fundamental side chains found on amino acids, for example, lysine, arginine, aspartic corrosive or glutamic corrosive or originate from metal cofactors, for example, zinc. Metal particles are especially viable and can lessen the pKa of water enough to make it a successful nucleophile.
Orderly PC reenactment concentrates set up that electrostatic impacts give, by a long shot, the biggest commitment to catalysis
====================================================
Q 21
Answer C.
serine 195,
histidine 57,
and aspartate 102
Q 22
Of all thespecies that enzymes bind, they are thought to bind most tightly ...
Answer
C) transition states
Q 23
In the chymotrypsin mechanism, what is used to stabilize the negative charge on the carbonyl oxygen of the transition state
Answer
A) hydrogen bonding between the enzyme and the anion from the carbonyl oxygen
Q 24
The ability for an enzyme to change its shape upon substrate binding represents the concept of ___
Answer
b) induced fit
Q 25
The enzyme hexokinase catalyzes a reaction where its substrates are completely sequesteredfrom the aqueous environment allowing for interactions to occur between enzyme and substratesthat would not normally occur in an aqueous environment.
What term describes this type of catalysis?
Answer
A) electrostatic catalysis
catalytic triad : it is a set of three is a gathering of three amino acids that are found in the dynamic locales of a few proteases required in catalysis.
Three distinct proteases that have reactant groups of three are: chymotrypsin, trypsin and elastase. In chymotrypsin, the reactant set of three is produced using serine 195, histidine 57, and aspartate 102. The side chain of serine is clung to the imidazole ring of the histidine deposit which acknowledges a proton from serine to shape a solid alkoxide nucleophile within the sight of a substrate for assault. The aspartate deposit situates histidine to improve it a proton acceptor by means of hydrogen holding and electrostatic responses.
=========================================
induced fit model: it is a proposed instrument of collaboration between a protein and a substrate. It proposes that introduction of a compound to a substrate causes the dynamic site of the catalyst to change shape with a specific end goal to permit the protein and substrate to tie (see enzyme–substrate complex).
===================================================
Electrostatic catalysis
Adjustment of charged move states can likewise be by buildups in the dynamic site shaping ionic bonds (or halfway ionic charge associations) with the middle of the road. These bonds can either originate from acidic or fundamental side chains found on amino acids, for example, lysine, arginine, aspartic corrosive or glutamic corrosive or originate from metal cofactors, for example, zinc. Metal particles are especially viable and can lessen the pKa of water enough to make it a successful nucleophile.
Orderly PC reenactment concentrates set up that electrostatic impacts give, by a long shot, the biggest commitment to catalysis
====================================================
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