Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Question
Chapter 26, Problem 13P
Interpretation Introduction
Interpretation:
A description about the subunit organization of ATCase from a functional point of view.
Concept introduction:
ATCase has six of every monetary unit, creating it hexameric. Therefore, ATcase is functionally a hexamer of
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
Serine protease enzyme mutation
To show differences in the effect of the nucleophilic attack of the carbonyl group (C=O) of peptide bond between the catalytic triad of serine, histidine and aspartic acid, and another catalytic triad contains alanine, histidine and aspartic acid
Provide/ draw an example of catalytic mechanism with catalytic triad contains alanine, histidine and aspartic
Please answer completely will give rating surely
protease mechanism:
you isolate a new protease which cleaves the peptide bond 2 aa residues before a
F residue. You might expect to fınd...
O An I residue in the S2'pocket
AL residue in the S2 pocket
O aV residue in the oxyanion hole
An Lresidue in the catalytic triad
in Michaelis-Menton kinetics, cutting the enzyme concentration in half will
O will double the reaction rate
O will not change Vo and Vmax
will change Vo but not turnover number
decrease Km by half
Fozyme Action: An Investigation of Lactase Activity
137
PART F EFFECT OF pH ON ENZYME ACTIVITY
Activity of Lactaid at Several pls
Observation with Tes Tape"
Glucose present?
Lactose
90 change
More Grean tello
Green Hellow
NO change
Green
NO
pH 7
Yes, 100 mgloL
pH 2
Yes
7100 mglaL
pH 10
NO
Glucose
tes 300 mglaL
RART G. EFFECT OF AN INHIBITOR ON ENZYME ACTIVITY
Inhibitor Effects
Observation with Tes Tape
Glucose present?
Light Green
Teal
Yellow IGreen
Dark Brown
Lactose
Yes
Lactaid"
NO
Ethanol
Yes
Yes
Glucose
1. What is the optimum pH of the lactose-conversion reaction, as shown by your data?
2 Did ethanol act as an efficient inhibitor of the lactose conversion to glucose and galactose?
3. Summarize your findings about the concentration, temperature, and pH sensititivity of lactase.
Chapter 26 Solutions
Biochemistry
Ch. 26 - Prob. 1PCh. 26 - Prob. 2PCh. 26 - Allosteric Regulation of Purine and Pyrimidine...Ch. 26 - Inhibition of Purine and Pyrimidine Metabolism by...Ch. 26 - Prob. 5PCh. 26 - Allosteric Regulation of Ribonucleotide Reductase...Ch. 26 - Prob. 7PCh. 26 - Prob. 8PCh. 26 - Prob. 9PCh. 26 - Prob. 10P
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- Biosynthesis of fatty acid 20:D6 from acetyl-CoA occurs in the __________ of mammalian cells. Cytosol Endoplasmic reticulum Both A and B Neither A nor B Assuming all three carbon atoms of glycerol are labeled as C14 radioisotopes and the radioisotope-labeled glycerol undergoes metabolism in animals. All of the following molecules in the animal maycontain C14 radioisotopes EXCEPT: Pyruvate Acetyl-CoA Glutamine Fatty acids Oxaloacetate All of the above molecules may contain C14 radioisotopearrow_forwardThe allosteric site 1). Draw a representation of an allosteric binding site of an enzyme. must bind an allosteric modifier that maintains three hydrophobic regions, a polar charged region and two regions of hydrogen bonding. You choose the order or organization of the characteristics in the allosteric site - label all regions. Details the allosteric site is composed of faces of two separate beta sheets and two separate alpha helices. You might decide that each beta sheet or each alpha helix contributes one amino acid R group to the allosteric site or you may decide that one of the beta sheets or one of the alpha helixes contributes two or more amino acid R groups to the allosteric organization. Your choice but please show R group structure in the allosteric site!arrow_forwardI don't understand it. Can u help me? Can u help me to explain this to me, pleasearrow_forward
- Regulation of Glutamine Synthetase by Covalent Modification Suppose at certain specific metabolite concentrations in vivo the cyclic cascade regulating E. coli glutamine synthetase has reached a dynamic equilibrium where the average state of GS adenylylation is poised atn=6. Predict what change in nwill occur if: [ ATP ] increases, PIIA/PIID increases, [ -KG ]/[ Gln ] increases, [ Pi ] decreases.arrow_forwardbiosynthesis of Thymidine monophosphate from ATP, HCO3-, Gln, Asp, quinone, and methylene THF. Show your work and don’t forget that the conversion of U to T only happens AFTER Ribonucleotide Reductase processes the 2’, 3’ ribose to the 3’ deoxy ribosearrow_forwardChemical labeling of chymotrypsin by the compound tosylphenylalanine chloromethyl ketone (TPCK) modifies the His 57 in the enzyme's active site. The structure of this derivative is shown below. TPCK inactivates the enzyme because the bulky addition prevents it from cleaving nearby covalent bonds. HCI + CH, C-O Chymotrypsin-His 57 TPCK Modified enzyme True O Falsearrow_forward
- #1 Specify the role each of the following amino acids play within the crystal structure and/or active site for Be as specific as possible, with pictures (and mechanistic arrows) as necessary. His11 Arg140 Glu89 Trp68 #2 Provide a step-wise mechanism for the reaction Bisphosphoglycerate mutase catalyzes, using the amino acids responsible for aiding in catalysis. You do not need to add surrounding amino acids that aid in substrate specificity. (drawn out)arrow_forwardPlz answer correctly do not copy. Question- Arsinate binds to reduced thio groups such as those found in cystiene residues in proteins, lipoate or glutathione. The resulting inhibition leads to central nervous system pathologies. The binding of arsinate to the dihydrolipoyl groups inhibits which of the following enzyme(s)? succinate dehydrogenase malate dehydrogenase pyruvate dehydrogenase complex branched-chain amino acid dehydrogenase complex isocitrate dehydrogenase alpha-ketoglutarate dehydrogenase complexarrow_forwardM-CSA Mechanism and Catalytic Site Atlas (ebi.ac.uk) (ii) Acyl Carrier Protein S-acetyltransferase (EC 2.3.1.38) is a transferase enzyme that catalyzes the first biosynthetic pathway for fatty acid synthase. It transfers the acyl group (CH3CO) first from coenzyme A to a cysteine residue in the active site. This is similar to what happens in Chymotrypsin, however utilizing a sulfur instead of an oxygen. The acyl group is then transferred to the molecule ACP. Provide the enzyme- catalyzed mechanism for the reaction below, making sure to identify the roles of all key amino acids: i H3C SCOA acetyl COA enzyme + HS i H3C SACP acetyl ACParrow_forward
- Number 2 please thank youarrow_forwardNeed both parts answeredarrow_forwardLysozyme’s use of aspartic acid and glutamic acid, to break the glycosidic bonds of the eubacterial cell wall (composed of peptidoglycan), illustrates the common enzymatic pattern of: hydrolysis (catabolic), using nonpolar amino acids at the active site hydrolysis (catabolic), using polar amino acids at the active site condensation (anabolic), using nonpolar amino acids at the active site condensation (anabolic), using polar amino acids at the active site all of the abovearrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Macromolecules | Classes and Functions; Author: 2 Minute Classroom;https://www.youtube.com/watch?v=V5hhrDFo8Vk;License: Standard youtube license