On the Multiple Functional Roles of the Active Site Histidine in Catalysis and Allosteric Regulation ofEscherichia coliGlucosamine 6-Phosphate Deaminase†

Biochemistry ◽  
2001 ◽  
Vol 40 (34) ◽  
pp. 10187-10196 ◽  
Author(s):  
Gabriela M. Montero-Morán ◽  
Samuel Lara-González ◽  
Laura I. Álvarez-Añorve ◽  
Jacqueline A. Plumbridge ◽  
Mario L. Calcagno
Keyword(s):  
Active Site ◽  
Allosteric Regulation ◽  
Functional Roles ◽  
Active Site Histidine

Identification of an active site histidine in urokinase

1976 ◽  
Vol 429 (1) ◽  
pp. 252-257 ◽  
Author(s):  
Eng Bee Ong ◽  
Alan J. Johnson ◽  
Guenther Schoellmann
Keyword(s):  
Active Site ◽  
Active Site Histidine

scholarly journals Phospholipase A2 Engineering. Structural and Functional Roles of the Highly Conserved Active Site Residue Aspartate-49

Biochemistry ◽  
1994 ◽  
Vol 33 (49) ◽  
pp. 14714-14722 ◽  
Author(s):  
Yishan Li ◽  
Bao-Zhu Yu ◽  
Hongxin Zhu ◽  
Mahendra K. Jain ◽  
Ming-Daw Tsai
Keyword(s):  
Phospholipase A2 ◽  
Active Site ◽  
Active Site Residue ◽  
Functional Roles

scholarly journals The location of the active-site histidine residue in the primary sequence of papain

1968 ◽  
Vol 108 (5) ◽  
pp. 861-866 ◽  
Author(s):  
S. S. Husain ◽  
G. Lowe
Keyword(s):  
Amino Acid ◽  
Sodium Borohydride ◽  
Active Site ◽  
Iodoacetic Acid ◽  
Cysteine Residue ◽  
Histidine Residue ◽  
Primary Sequence ◽  
Active Site Cysteine ◽  
Active Site Histidine ◽  
Active Site Cysteine Residue

Papain that had been irreversibly inhibited with 1,3-dibromo[2−14C]acetone was reduced with sodium borohydride and carboxymethylated with iodoacetic acid. After digestion with trypsin and α-chymotrypsin the radioactive peptides were purified chromatographically. Their amino acid composition indicated that cysteine-25 and histidine-106 were cross-linked. Since cysteine-25 is known to be the active-site cysteine residue, histidine-106 must be the active-site histidine residue.

Allosteric theory

Hemoglobin ◽  
2018 ◽  
pp. 42-57
Author(s):  
Jay F. Storz
Keyword(s):  
Active Site ◽  
Binding Sites ◽  
Allosteric Regulation ◽  
Theoretical Models ◽  
State Model ◽  
Regulatory Control ◽  
Indirect Interaction ◽  
Protein Activity ◽  
Conformational States ◽  
Two State Model

Chapter 3 provides a brief overview of allostery, the modulation of protein activity that is caused by an indirect interaction between structurally remote binding sites. In this mode of intramolecular regulatory control, the binding of ligand at a protein’s active site is influenced by the binding of another ligand at a different site in the same protein. This interaction at a distance is mediated by a ligation-induced transition between alternative conformational states. Hemoglobin is regarded as the “allosteric paradigm,” and the oxygenation-linked transition between alternative quaternary conformations provides a textbook example of how allostery works. This chapter reviews different theoretical models, such as the Monod-Wyman-Changeux “two-state” model, to explain the allosteric regulation of hemoglobin function.

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