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Science 22 September 1995:
Vol. 269. no. 5231, pp. 1684 - 1691
DOI: 10.1126/science.7569894
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Articles

Science, Vol 269, Issue 5231, 1684-1691
Copyright © 1995 by American Association for the Advancement of Science

articles

Vitamin K and energy transduction: a base strength amplification mechanism

P Dowd, R Hershline, SW Ham, and S Naganathan

Department of Chemistry, University of Pittsburgh, PA 15260, USA.

Energy transfer provides an arrow in the metabolism of living systems. Direct energetic coupling of chemical transformations, such that the free energy generated in one reaction is channeled to another, is the essence of energy transfer, whereas the purpose is the production of high-energy chemical intermediates. Vitamin K provides a particularly instructive example of energy transfer. A key principle at work in the vitamin K system can be termed "base strength amplification." In the base strength amplification sequence, the free energy of oxygenation of vitamin K hydroquinone (vitamin KH2) is used to transform a weak base to a strong base in order to effect proton removal from selected glutamate (Glu) residues in the blood-clotting proteins.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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PNAS 103, 19308-19313
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J. S. Johnson, B. A. Soute, C. S. Olver, and D. C. Baker (2006)
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Vet. Pathol. 43, 430-437
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Vitamin K epoxide reductase significantly improves carboxylation in a cell line overexpressing factor X.
Y.-M. Sun, D.-Y. Jin, R. M. Camire, and D. W. Stafford (2005)
Blood 106, 3811-3815
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The Vitamin K-dependent Carboxylase Has Been Acquired by Leptospira Pathogens and Shows Altered Activity That Suggests a Role Other than Protein Carboxylation.
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Engineering of a Recombinant Vitamin K-dependent {gamma}-Carboxylation System with Enhanced {gamma}-Carboxyglutamic Acid Forming Capacity: EVIDENCE FOR A FUNCTIONAL CXXC REDOX CENTER IN THE SYSTEM.
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J. Biol. Chem. 280, 10540-10547
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Chemical Modification of Cysteine Residues Is a Misleading Indicator of Their Status as Active Site Residues in the Vitamin K-dependent {gamma}-Glutamyl Carboxylation Reaction.
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A new model for vitamin K-dependent carboxylation: The catalytic base that deprotonates vitamin K hydroquinone is not Cys but an activated amine.
M. A. Rishavy, B. N. Pudota, K. W. Hallgren, W. Qian, A. V. Yakubenko, J.-H. Song, K. W. Runge, and K. L. Berkner (2004)
PNAS 101, 13732-13737
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A Conserved Region of Human Vitamin K-dependent Carboxylase between Residues 393 and 404 Is Important for Its Interaction with the Glutamate Substrate.
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J. Biol. Chem. 278, 46488-46493
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Determination of Disulfide Bond Assignment of Human Vitamin K-dependent {gamma}-Glutamyl Carboxylase by Matrix-assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry.
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J. Biol. Chem. 278, 45468-45475
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Identification of Sequences within the gamma -Carboxylase That Represent a Novel Contact Site with Vitamin K-dependent Proteins and That Are Required for Activity.
B. N. Pudota, E. L. Hommema, K. W. Hallgren, B. A. McNally, S. Lee, and K. L. Berkner (2001)
J. Biol. Chem. 276, 46878-46886
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Identification of the vitamin K-dependent carboxylase active site: Cys-99 and Cys-450 are required for both epoxidation and carboxylation.
B. N. Pudota, M. Miyagi, K. W. Hallgren, K. A. West, J. W. Crabb, K. S. Misono, and K. L. Berkner (2000)
PNAS 97, 13033-13038
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The Vitamin K-Dependent Carboxylase.
K. L. Berkner (2000)
J. Nutr. 130, 1877-1880
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A topological study of the human gamma -glutamyl carboxylase.
J. Tie, S.-M. Wu, D. Jin, C. V. Nicchitta, and D. W. Stafford (2000)
Blood 96, 973-978
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Calcium binding mode of {gamma}-carboxyglutamic acids in conantokins.
C.H. Lin, F.C.H. Chan, J.K. Hwang, and P.C. Lyu (1999)
Protein Eng. Des. Sel. 12, 589-595
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Vitamin K-Dependent Biosynthesis of gamma -Carboxyglutamic Acid.
B. Furie, B. A. Bouchard, and B. C. Furie (1999)
Blood 93, 1798-1808
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Propeptide and glutamate-containing substrates bound to the vitamin K-dependent carboxylase convert its vitamin K epoxidase function from an inactive to an active state.
I. Sugiura, B. Furie, C. T. Walsh, and B. C. Furie (1997)
PNAS 94, 9069-9074
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From the Cover: gamma -Glutamyl carboxylation: An extracellular posttranslational modification that antedates the divergence of molluscs, arthropods, and chordates.
P. K. Bandyopadhyay, J. E. Garrett, R. P. Shetty, T. Keate, C. S. Walker, and B. M. Olivera (2002)
PNAS 99, 1264-1269
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