Structure and mechanism in the enzymic activity of carboxypeptidase A and relations to chemical sequence
About: This article is published in Accounts of Chemical Research.The article was published on 1970-03-01. It has received 126 citations till now. The article focuses on the topics: Carboxypeptidase A & Carboxypeptidase.
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TL;DR: The dynamics of a folded globular protein have been studied by solving the equations of motion for the atoms with an empirical potential energy function and suggest that the protein interior is fluid-like in that the local atom motions have a diffusional character.
Abstract: The dynamics of a folded globular protein (bovine pancreatic trypsin inhibitor) have been studied by solving the equations of motion for the atoms with an empirical potential energy function. The results provide the magnitude, correlations and decay of fluctuations about the average structure. These suggest that the protein interior is fluid-like in that the local atom motions have a diffusional character.
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01 Jan 1981TL;DR: The Internal Dynamics of Globular Protein (IDGP) as mentioned in this paper is a well-known model for the internal dynamics of protein structures and its dynamics in the context of protein synthesis.
Abstract: (1981). The Internal Dynamics of Globular Protein. Critical Reviews in Biochemistry: Vol. 9, No. 4, pp. 293-349.
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TL;DR: This chapter discusses the relationship of the three-dimensional structures of bovine carboxypeptidase A, and of its complexes with substrates and inhibitors, to the functional behavior of this enzyme.
Abstract: Publisher Summary This chapter discusses the relationship of the three-dimensional structures of bovine carboxypeptidase A (CPA), and of its complexes with substrates and inhibitors, to the functional behavior of this enzyme. In particular, it discusses the basis for substrate specificity, modes of binding, and possible mechanisms of hydrolytic cleavage of substrates for this enzyme. CPA is a zinc-containing proteolytic enzyme, which catalyzes the hydrolysis of carboxy-terminal peptide bonds in protein and peptide substrates. Removal of Zn2+, either by lowering the pH below 5.5 or by the use of a variety of chelating agents at neutral pH, yields an inactive enzyme, apocarboxypeptidase A. Peptidase activity is known for Co2+, Ni2+, Mn2+ and Fe2+ in place of Zn2+, but substitution of Cu2+ for Zn2+ yields an enzyme that is inactive toward all substrates. Esters are also cleaved by CPA and the substitution of Hg2+, Cd2+, or Pb2+ retains esterase activity, although these heavy metal derivatives are not peptidases in solution. However, the crystals of the mercury derivative have shown some peptidase activity.
352 citations
References
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TL;DR: Structure of Hen Egg-White Lysozyme: A Three-dimensional Fourier Synthesis at 2 A Resolution as mentioned in this paper, 3D Fourier synthesis at 2 a resolution.
Abstract: Structure of Hen Egg-White Lysozyme: A Three-dimensional Fourier Synthesis at 2 A Resolution
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TL;DR: A three-dimensional X-ray study at a resolution of 2.8 A has revealed that the single polypeptide chain of 211 residues is folded into two distinct parts which are divided by a cleft as mentioned in this paper.
Abstract: A three-dimensional X-ray study at a resolution of 2.8 A has revealed that the single polypeptide chain of 211 residues is folded into two distinct parts which are divided by a cleft. The active site, consisting of a cysteine and a histidine, lies at the surface of the cleft. Apart from four short α-helical segments and one short segment of β-structure, the conformation of the chain is irregular.
450 citations