Literature DB >> 7569894

Vitamin K and energy transduction: a base strength amplification mechanism.

P Dowd1, R Hershline, S W Ham, S Naganathan.   

Abstract

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.

Entities:  

Mesh：

Substances：

Year:  1995        PMID： 7569894     DOI： 10.1126/science.7569894

Source DB:  PubMed          Journal:  Science        ISSN： 0036-8075            Impact factor:   47.728


  22 in total

1.  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.

Authors:  I Sugiura; B Furie; C T Walsh; B C Furie
Journal:  Proc Natl Acad Sci U S A       Date:  1997-08-19       Impact factor: 11.205

2.  Identification of the N-linked glycosylation sites of vitamin K-dependent carboxylase and effect of glycosylation on carboxylase function.

Authors:  Jian-Ke Tie; Mei-Yan Zheng; R Marshall Pope; David L Straight; Darrel W Stafford
Journal:  Biochemistry       Date:  2006-12-12       Impact factor: 3.162

3.  gamma -Glutamyl carboxylation: An extracellular posttranslational modification that antedates the divergence of molluscs, arthropods, and chordates.

Authors:  Pradip K Bandyopadhyay; James E Garrett; Reshma P Shetty; Tyler Keate; Craig S Walker; Baldomero M Olivera
Journal:  Proc Natl Acad Sci U S A       Date:  2002-01-29       Impact factor: 11.205

Review 4.  Enzymatic chemistry of cyclopropane, epoxide, and aziridine biosynthesis.

Authors:  Christopher J Thibodeaux; Wei-chen Chang; Hung-wen Liu
Journal:  Chem Rev       Date:  2011-10-21       Impact factor: 60.622

5.  Antibacterial Strategy against H. pylori: Inhibition of the Radical SAM Enzyme MqnE in Menaquinone Biosynthesis.

Authors:  Sumedh Joshi; Dmytro Fedoseyenko; Nilkamal Mahanta; Rodrigo G Ducati; Mu Feng; Vern L Schramm; Tadhg P Begley
Journal:  ACS Med Chem Lett       Date:  2019-02-15       Impact factor: 4.345

6.  Mechanism of MenE inhibition by acyl-adenylate analogues and discovery of novel antibacterial agents.

Authors:  Joe S Matarlo; Christopher E Evans; Indrajeet Sharma; Lubens J Lavaud; Stephen C Ngo; Roger Shek; Kanagalaghatta R Rajashankar; Jarrod B French; Derek S Tan; Peter J Tonge
Journal:  Biochemistry       Date:  2015-10-15       Impact factor: 3.162

7.  A hetero-dimer model for concerted action of vitamin K carboxylase and vitamin K reductase in vitamin K cycle.

Authors:  Sangwook Wu; Shubin Liu; Charles H Davis; Darrel W Stafford; John D Kulman; Lee G Pedersen
Journal:  J Theor Biol       Date:  2011-03-29       Impact factor: 2.691

8.  Identification of the vitamin K-dependent carboxylase active site: Cys-99 and Cys-450 are required for both epoxidation and carboxylation.

Authors:  B N Pudota; M Miyagi; K W Hallgren; K A West; J W Crabb; K S Misono; K L Berkner
Journal:  Proc Natl Acad Sci U S A       Date:  2000-11-21       Impact factor: 11.205

9.  A new model for vitamin K-dependent carboxylation: the catalytic base that deprotonates vitamin K hydroquinone is not Cys but an activated amine.

Authors:  Mark A Rishavy; B Nirmala Pudota; Kevin W Hallgren; Wen Qian; Anna V Yakubenko; Jee-Hyeon Song; Kurt W Runge; Kathleen L Berkner
Journal:  Proc Natl Acad Sci U S A       Date:  2004-09-13       Impact factor: 11.205

10.  Insight into the coupling mechanism of the vitamin K-dependent carboxylase: mutation of histidine 160 disrupts glutamic acid carbanion formation and efficient coupling of vitamin K epoxidation to glutamic acid carboxylation.

Authors:  Mark A Rishavy; Kathleen L Berkner
Journal:  Biochemistry       Date:  2008-08-22       Impact factor: 3.162
View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.