Describe the specificity of aminotransferases for their substrates.
Answer:-
Aminotransferases or transaminases are a group of enzymes that catalyze the interconversion of amino acids and oxoacids by transfer of amino groups. Aspartate aminotransferase (AST), formerly termed glutamate oxaloacetate transaminase (GOT), and alanine aminotransferase (ALT), formerly termed glutamate pyruvate transaminase (GPT), are the two aminotransferases of greatest clinical significance.
The specificity of individual enzymes determines the specific amino acid that serves as the other amino group donor. In the AST reaction, the l-amino acid is aspartate; for ALT, it is alanine.
aconitase produces only one of the isocitrate stereoisomers.Which of the following terms describe the specificity of aconitase, absolute specificity,relative specificity,stereospecificity?
describe the three stages of aerobic glucose catabolism including their substrates, products and net energy production.
Describe 2 reasons why the DNA major groove offers more specificity for protein binding.
Most enzymes are quite specific, catalyzing a particular reaction on a set of substrates that are structurally quite similar to one another. Discuss why this is advantageous from a biological perspective. Suggest why this is likely to be true from a chemical perspective. That is, why would it be difficult to evolve an enzyme with high catalytic activity but low specificity?
CI OD 17) Human alcohol dehydrogenase is capable of oxidizing several substrates besides ethanol. The kinetic parameters for these other substrates are given in the table below. Assume a constant enzyme amount of 1 mmol when these experimental values were obtained Use this table to answer questions 17a and 17b. note:UM = micromolar Substrate Km (UM) Vmax (mmol/min) Hexanol Butanol Ethylene Glycol Methanol Propanol UTA 17a) Which is the most preferred substrate according to these values? Question 33 4 pts...
Epoxides and oxetanes as substrates model of the reactant molecule. 10.7 Epoxides and Oxetanes as Substrates 10.52 For each reaction, draw the complete, detailed mechanism and the major product. NaCl HCI
Join borosilicate glass substrates containing a-SiC:H films with substrates containing titanium films. This will be done by activating the surface of the wafers with APTMS ((3-Aminopropyl) trimethoxysilane) to subsequently bind these molecules with glutaraldehyde. ¿How can I improve biofunctionalization between APTMS ((3- Aminopropyl) trimethoxysilane) and glutaraldehyde?
Which of the following is true for simultaneous testing? a. Net specificity is greater than the specificity of either test alone b. Net specificity is less than the specificity of either test alone c. Net specificity is the same as that of the more specific test d. Net specificity is the same as that of the less specific test
I have calculated sensitivity, specificity, PPV, NPV, LR(+), and LR(-) for the test below. My question is how to describe the test, i.e. good/bad, any features to notice? Condition Present Condition Absent Total Test + 83 8 91 Test - 6 22 28 Total 89 30 119 Sensitivity = 0.93 Specificity = 0.73 PPV = 0.91 NPV = 0.79 LR(+) = 3.44 LR(-) = 0.095
how does the specificity change? Substrate Specificity Example 2: Proteases Proteases - cleave peptide bonds Ami Componcnt Thrombin (only Arg-Gly bonds) Trypsin (Arg-X, or Lys-X bonds) Subtilisin (X-X) Howdoes the specifity change gingdo the sare