Enzyme Assignement 2
1. A) I would expect the active site of nylonase to consist mainly of polar amino acids with a few nonpolar amino acids as well because the substrate for nylonase is polar overall, but has many nonpolar bonds. What makes me think that the nylonase enzyme is polar is that the substrate that would bind to the active site of nylonase has extreme polarity between carbon and oxygen, and between hydrogen and nitrogen due to their differences in electronegativity’s, but it still has the nonpolar bonds between carbons and hydrogens. Polar amino acids bond with polar substrates and nonpolar amino acids bond with nonpolar substrates and because of this and the fact that nylonase is polar overall I would expect more polar amino acids to attract, but I would still expect some nonpolar amino acids to attract because of all of the nonpolar carbon-hydrogen bonds.
B) Glycine structure: H3N+-- C—C—O- Glycine Dipeptide: N—C—C—N—C—C—O
I believe that a dipeptide with two glycine molecules (glycylglycine) would be a competitive inhibitor of nylonase because it is polar with a few nonpolar bonds, it has a similar structure and it has a few common areas such as N bonded with H and C double bonded with O (which is where its polarity comes from). Because of how similar glycylglycine is to the nylon it would probably very easily bond to the nylonase enzyme that nylon would be a substrate to. It would be a competitive inhibitor because it would easily bond to the same place as the nylon substrate would in the enzyme instead of a different place which it would do if it was non-competitive due to all of its similarities.
2.
Maltose most likely acts as a competitive inhibitor to lactose because lactose is broken down by lactase at a much quicker rate without the presence of maltose. This shows that when maltose is present lactose is not being broken down quite as quickly meaning that it is an inhibitor to lactose. The reason for which
B) Glycine structure: H3N+-- C—C—O- Glycine Dipeptide: N—C—C—N—C—C—O
I believe that a dipeptide with two glycine molecules (glycylglycine) would be a competitive inhibitor of nylonase because it is polar with a few nonpolar bonds, it has a similar structure and it has a few common areas such as N bonded with H and C double bonded with O (which is where its polarity comes from). Because of how similar glycylglycine is to the nylon it would probably very easily bond to the nylonase enzyme that nylon would be a substrate to. It would be a competitive inhibitor because it would easily bond to the same place as the nylon substrate would in the enzyme instead of a different place which it would do if it was non-competitive due to all of its similarities.
2.
Maltose most likely acts as a competitive inhibitor to lactose because lactose is broken down by lactase at a much quicker rate without the presence of maltose. This shows that when maltose is present lactose is not being broken down quite as quickly meaning that it is an inhibitor to lactose. The reason for which