. The first two steps of ovothiol C biosynthesis are shown below. Propose the rest of the pathway, indicating the potential involve- ment of cofactors. co- coo H NH,* Histidine Fo*, 02 reductant .coo- *H,N° coo- *H,N° COO HS* NH,* 5-Histidylcysteine sulfoxide conjugate 5-Histidylcysteine thioether conjugate Cysteine

. The first two steps of ovothiol C biosynthesis are shown below. Propose the rest of the pathway, indicating the potential involve- ment of cofactors. co- coo H NH,* Histidine Fo, 02 reductant .coo- H,N° coo- H,N° COO HS NH,* 5-Histidylcysteine sulfoxide conjugate 5-Histidylcysteine thioether conjugate Cysteine

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter27: Metabolic Integration And Organ Specialization

Section: Chapter Questions

Problem 20P: Figure 27.3 illustrates the response of R (ATP-regenerating) and U (ATP-utilizing) enzymes to energy...

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Chart is Given for you: Below is a chart of values for actual enzymes. Enzyme Km (M) kcat (1/s)Chymotrypsin 1.5 × 10^−2 0.14Pepsin 3.0 × 10^−4 0.5Tyrosyl-tRNA synthetase 9.0 × 10^−4 7.6Ribonuclease 7.9 × 10^−3 7.9 × 10^2Carbonic anhydrase 2.6 × 10^−2 4.0 × 10^5Fumarase 5.0 × 10^−6 8.0 × 10^2 Assume the enzyme concentration is equal across all samples (and is equal to 1). (Answer a and b only)a. Which enzyme will have the highest V0 at very high substrate concentrations? (1 M). Why? b. Which will have the highest V0 at very low substrate concentrations (5.0 × 10^−12). Why?
Can someone help me answer non-graded bio questions pertaining to lactase I'm trying to understand it more?
1 ).Which of the following accurately describes substrate specificity for serine proteases? A.The binding cleft B.Mg2+ metal activated enzyme C.The catalytic triad D.Facilitates redox chemistry E.Stabilizes the transition state 2). Which of the following amino acid residues would not provide a side chain for acid-base catalysis at physiological pH? select all that apply leucine aspartic acid histidine lysine Please answer both correct i will give u upvote.
help fill in the word between brackets Serine proteases are an example of [nucleophilic/electrophilic/covalent/acid- base] catalysts because the catalytic triad [aspartate/serine/histidine] protonates the leaving group and abstracts a proton from water. Serine proteases are an example of [nucleophilic/electrophilic/covalent/acid-base] catalysts because the catalytic [aspartate/serine/histidine] is converted to an oxyanion to attack the peptide bond. Serine proteases are an example of [nucleophilic/electrophilic/covalent/acid-base] catalysts because an acyl-enzyme intermediate is formed during the catalytic cycle between part of the substrate and the catalytic [aspartate/serine/histidine].
Based on this graph, it appears that carboxylesterase is most active at a pH of A. 3.5B. 1.5C. 5D. 4
The steps of the chymotrypsin mechanisms are listed below (1-7). Put the steps of chymotrypsin mechanism in the correct order. Figure representing chymotrypsin mechanism is given for reference. a.The portion (N-terminal end) of original substrate with the new C terminus diffuses away b. Substrate binding c. His 57 catalyzes removal of H from Ser 195 hydroxyl; Ser 195’s nucleophilic O attacks carbonyl C of substrate; tetrahedral intermediate is formed d. Water binding; water is deprotonated by His 57; resulting OH nucleophilically attacks carbonyl of remaining substrate; tetrahedral intermediate is formed e. His 57 donates H to N of…
There are parts A-C for this picture included. A) What type of enzyme is Malate Dehydrogenase? choices: Hydrolase, Isomerase, Ligase, Oxideoreductase, Transferase, or Translocase B) Which of the following statements are true in biochemical standard conditions? There can be more than 1. Choices: The reaction is spontaneous since ∆G°' is positive The reaction is spontaneous since ∆G°' is negative The reaction is not spontaneous since ∆G°' is positive The reaction is not spontaneous since ∆G°' is positive The equilibrium favors products since K is greater than 1 The equilibrium favors reactants since K is greater than 1 The equilibrium favors products since K is less than 1 The equilibrium favors reactants since K is less than 1 The reaction is always at equilibrium C) If the concentration of Oxaloacetate is 10^7 times lower than the concentration of Malate D.,Is the reaction Spontanuous? Choices: No, because RTInQ is very positive Yes, because RTlnQ is very…
Match each of the enzymes involved in de novo pyrimidine synthesis with the correct description: _______ Dihydroorotate dehydrogenase _______ UMP synthase_______ Carbamoyl phosphate synthetase II _______ TMP synthase _______ CTP synthetase_______ Aspartate transcarbamoylase _______ PRPP synthetase (A) attaches an aspartate to an activated carbamoyl molecule(B) bifunctional enzyme that combines a nitrogenase pyrimidine ring to an activated ribose(C) catalyzes the formation of the activated ribose sugar(D) uses glutamine to add an amine to a preformed nucleotide(E) produces the first cyclic nitrogenase ring during de novo pyrimidine synthesis(F) combines bicarbonate and nitrogen from glutamine in the first step of pyrimidine ring synthesis (G) uses a folate derivative to add a methyl group to a preformed nucleotide
Lyases enzymes catalyzes removal of group from substrate by mechanism other than hydrolysis leaving double bond?
Sydney Brennen isolated Salmonella typhimurium mutants that were implicated in the biosynthesis of tryptophan and would not grow on minimal medium supplemented with intermediates in tryptophan biosynthesis, some mutants were able to grow while others remained unable to grow. Review the data attached to order the biosynthetic pathway by both enzymatic step and by intermediate biomolecule. Label the step impacted by each of the mutant cell lines.
1. Demonstrate your understanding whether carrier-free biocatalysts should or should not be considered as good biocatalysts. You discussion must be in detail and related to biocatalysis. You can provide detail explanation or provide example. 2. Compare and contrast the following pairs of terms. Relate their similarities and differences to applications in biocatalysis. Zymonomas sp. and Saccharomyces sp.
The key regulatory enzyme is purine synthesis is: a. Glycinamide ribonucleotide synthetase. b. Adenylosuccinate lyase. c. Glutamine phosphoribosyl amidotransferase. d. Carbamoyl phosphate synthetase.