EBK ORGANIC CHEMISTRY
EBK ORGANIC CHEMISTRY
6th Edition
ISBN: 8220103151757
Author: LOUDON
Publisher: MAC HIGHER
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Chapter 25, Problem 25.12P
Interpretation Introduction

Interpretation:

The curve arrow mechanism for the hydrolysis of phosphotyrosine esters in protein by enzyme catalysis with enzyme protein phosphotyrosine phosphatases including the structure of the phosphoenzyme intermediate is to be shown.

Concept Introduction:

In the hydrolysis of phosphotyrosine esters in protein proceed through phosphoenzyme intermediate formed by nucleophilic attack of thiol of cysteine residue, which is further on nucleophilic attack of water forms the phosphate.

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The molar absorptivity of a protein in water at 280 nm can be estimated within ~5-10% from its content of the amino acids tyrosine and tryptophan and from the number of disulfide linkages (R-S-S-R) between cysteine residues:   Ε280 nm (M-1 cm-1) ≈ 5500 nTrp + 1490 nTyr + 125 nS-S   where nTrp is the number of tryptophans, nTyr is the number of tyrosines, and nS-S is the number of disulfide linkages. The protein human serum transferrin has 678 amino acids including 8 tryptophans, 26 tyrosines, and 19 disulfide linkages. The molecular mass of the most dominant for is 79550.   Predict the molar absorptivity of transferrin. Predict the absorbance of a solution that’s 1.000 g/L transferrin in a 1.000-cm-pathlength cuvet. Estimate the g/L of a transferrin solution with an absorbance of 1.50 at 280 nm.
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