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].

Can someone please help me with these two questions, please hurry I only have 45 minutes;

1. Acid phosphatases are an important group of enzymes that can be detected in human bloodserum. Under slightly acidic conditions (pH 5.0), this group of enzymes can hydrolyzebiological phosphate esters as follows:R-O-P-O3-2 + H 2O
R-OH + HO-P-O3-2.Acid phosphatases are produced and can be detected in erythrocytes, kidney, spleen, the liver,and prostrate gland. The enzyme from the prostrate gland is clinically important because anincreased activity in the blood is frequently an indication of cancer of the prostrate gland.Tartrate ion can strongly inhibit the phosphatase from the prostrate gland, but not acidphosphatases from other tissues. How can you use the information above to develop a specificprocedure for measuring the activity of the acid phosphatase of the prostrate gland in humanblood serum?

8.Choose the False statement about enzyme binding sites Binding at an allosteric site ca affect binding and catalysis at the Ortho steric site. In addition to ortho steric sites , some enzymes have other sites where catalysis can be conducted. They are called , allosteric sites, from “allo,” the other. In principle, allosteric ligands can have structures that do not resemble those of substrates. Ligand binding at an allosteric site can cause a conformational change of an enzyme. Enzyme can be inhibited by an allosteric ligand that does not complete with substrate.

Please type answer note write by hend.

Can you please help solve this problem?

What kind of catalysis is cysteine driving in this picture? S Los i fy R……—NHR N-H---S O. N-H H-N H-N. O Metal catalysis Covalent catalysis Base catalysis O Acid catalysis NHR²

what does the Hexa protein domain depict? (in relation with tay sachs disease)

Can you please describe the specific components that each of these structures are comprised of ( alpha helices and beta sheets) in more detail? Also, what do the different colors represent?  Your reply will be greatly appreciated.  The ligand that was assigned to me is tadalafil.

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