Dec 1, 1973

Enzymatic activities of carobxypeptidase A's in solution and in crystals

Proceedings of the National Academy of Sciences of the United States of America
W N Lipscomb

Abstract

Activities of all known forms of bovine carboxypeptidase A's (alpha having 307, beta having 305, and gamma having 300 amino acids) are essentially the same in solution under given conditions. However, activities in the crystals differ. The A(alpha) crystals elongated along the a axis (a) have unit cell parameters a = 51.41 A, b = 59.89 A, c = 47.19 A, and beta = 97 degrees 35', (b) show about [unk] of the activity of the dissolved enzyme, and (c) have the same color of the arsanilazo Tyr 248 derivative in the crystalline and solution states, namely red at pH 8.2 and yellow at pH 7.4. The A(gamma) crystals elongated along the b axis (a) have unit cell parameters a = 50.9 A, b = 57.9 A, c = 45.0 A, and beta = 94 degrees 40', (b) show [unk] of the activity of the dissolved enzyme, and (c) show, in the arsanilazo Tyr 248 derivative, yellow crystals and red solution at pH 8.2. Although the detailed three-dimensional structure is known for the A(alpha) form described above, the structure of the A(gamma) form is as yet undertermined. A reasonable hypothesis is that the major part of the differences in crystal behaviors is due to differences in intermolecular (crystal-packing) interactions. In particular the movement of Tyr 248 may be ...Continue Reading

  • References8
  • Citations13

References

  • References8
  • Citations13

Citations

Mentioned in this Paper

CPA1
Carboxypeptidase A
Crystal - Body Material
Structure-Activity Relationship
Amino Acids, I.V. solution additive
Electron Density
Bos taurus
Carboxypeptidase A Activity
X-Ray Diffraction
Zinc

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