Thrombin A-Chain: Activation Remnant or Allosteric Effector?

Thrombin A-Chain: Activation Remnant or Allosteric Effector?

Although prothrombin is one of the most widely studied enzymes in biology, the role of the thrombin A-chain has been neglected in comparison to the other domains. This paper summarizes the current data on the prothrombin catalytic domain A-chain region and the subsequent thrombin A-chain. Attention...

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Main Authors: Carter, Isis S. R., Vanden Hoek, Amanda L., Pryzdial, Edward L. G., MacGillivray, Ross T. A.
Format: Online
Language:English
Published: Hindawi Publishing Corporation 2010
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3211113/
id pubmed-3211113
recordtype oai_dc
spelling pubmed-32111132011-11-14 Thrombin A-Chain: Activation Remnant or Allosteric Effector? Carter, Isis S. R. Vanden Hoek, Amanda L. Pryzdial, Edward L. G. MacGillivray, Ross T. A. Review Article Although prothrombin is one of the most widely studied enzymes in biology, the role of the thrombin A-chain has been neglected in comparison to the other domains. This paper summarizes the current data on the prothrombin catalytic domain A-chain region and the subsequent thrombin A-chain. Attention is given to biochemical characterization of naturally occurring prothrombin A-chain mutations and alanine scanning mutants in this region. While originally considered to be simply an activation remnant with little physiologic function, the thrombin A-chain is now thought to play a role as an allosteric effector in enzymatic reactions and may also be a structural scaffold to stabilize the protease domain. Hindawi Publishing Corporation 2010 2010-12-09 /pmc/articles/PMC3211113/ /pubmed/22084659 http://dx.doi.org/10.1155/2010/416167 Text en Copyright © 2010 Isis S. R. Carter et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Carter, Isis S. R.
Vanden Hoek, Amanda L.
Pryzdial, Edward L. G.
MacGillivray, Ross T. A.
spellingShingle Carter, Isis S. R.
Vanden Hoek, Amanda L.
Pryzdial, Edward L. G.
MacGillivray, Ross T. A.
Thrombin A-Chain: Activation Remnant or Allosteric Effector?
author_facet Carter, Isis S. R.
Vanden Hoek, Amanda L.
Pryzdial, Edward L. G.
MacGillivray, Ross T. A.
author_sort Carter, Isis S. R.
title Thrombin A-Chain: Activation Remnant or Allosteric Effector?
title_short Thrombin A-Chain: Activation Remnant or Allosteric Effector?
title_full Thrombin A-Chain: Activation Remnant or Allosteric Effector?
title_fullStr Thrombin A-Chain: Activation Remnant or Allosteric Effector?
title_full_unstemmed Thrombin A-Chain: Activation Remnant or Allosteric Effector?
title_sort thrombin a-chain: activation remnant or allosteric effector?
description Although prothrombin is one of the most widely studied enzymes in biology, the role of the thrombin A-chain has been neglected in comparison to the other domains. This paper summarizes the current data on the prothrombin catalytic domain A-chain region and the subsequent thrombin A-chain. Attention is given to biochemical characterization of naturally occurring prothrombin A-chain mutations and alanine scanning mutants in this region. While originally considered to be simply an activation remnant with little physiologic function, the thrombin A-chain is now thought to play a role as an allosteric effector in enzymatic reactions and may also be a structural scaffold to stabilize the protease domain.
publisher Hindawi Publishing Corporation
publishDate 2010
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3211113/
_version_ 1611486059402625024

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