Loading…
The catalytic mechanism of nucleoside diphosphate kinases
Nucleoside diphosphate kinases catalyze the reversible transfer of the gamma phosphate of nucleoside triphosphates to nucleoside diphosphates. This minireview presents recent advances in understanding the reaction mechanism using steady-state and fast kinetic studies, X-ray crystallography, and site...
Saved in:
Published in: | Journal of bioenergetics and biomembranes 2000-06, Vol.32 (3), p.237 |
---|---|
Main Authors: | , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that cite this one |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
cited_by | cdi_FETCH-LOGICAL-c280t-39ad6e9335954d9802845c85aeec920361ea9b8c5201ead6c0597c60bd7d2d533 |
---|---|
cites | |
container_end_page | |
container_issue | 3 |
container_start_page | 237 |
container_title | Journal of bioenergetics and biomembranes |
container_volume | 32 |
creator | Lascu, I Gonin, P |
description | Nucleoside diphosphate kinases catalyze the reversible transfer of the gamma phosphate of nucleoside triphosphates to nucleoside diphosphates. This minireview presents recent advances in understanding the reaction mechanism using steady-state and fast kinetic studies, X-ray crystallography, and site-directed mutagenesis. We also briefly discuss the physiological relevance of in vitro studies. |
doi_str_mv | 10.1023/A:1005532912212 |
format | article |
fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_proquest_journals_758943309</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2166021341</sourcerecordid><originalsourceid>FETCH-LOGICAL-c280t-39ad6e9335954d9802845c85aeec920361ea9b8c5201ead6c0597c60bd7d2d533</originalsourceid><addsrcrecordid>eNo1jztPwzAUhS0EoqEws6GIPXDtmxvbbFXFS6rEUiS2yLVvlZTmQZwM_fdUokznDJ--oyPErYQHCQofF08SgAiVlUpJdSYSSRqzwhh5LhKQOWW5tl8zcRXjDgAMEFyKmZS6MAg6EXZdcerd6PaHsfZpw75ybR2btNum7eT33MU6cBrqvupiX7mR0--6dZHjtbjYun3km1POxefL83r5lq0-Xt-Xi1XmlYExQ-tCwRaRLOXBGlAmJ2_IMXurAAvJzm6MJwXHFgoPZLUvYBN0UIEQ5-L-z9sP3c_EcSx33TS0x8lSk7E5ItgjdHeCpk3DoeyHunHDofw_ir8sw1PG</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>758943309</pqid></control><display><type>article</type><title>The catalytic mechanism of nucleoside diphosphate kinases</title><source>Springer Nature</source><creator>Lascu, I ; Gonin, P</creator><creatorcontrib>Lascu, I ; Gonin, P</creatorcontrib><description>Nucleoside diphosphate kinases catalyze the reversible transfer of the gamma phosphate of nucleoside triphosphates to nucleoside diphosphates. This minireview presents recent advances in understanding the reaction mechanism using steady-state and fast kinetic studies, X-ray crystallography, and site-directed mutagenesis. We also briefly discuss the physiological relevance of in vitro studies.</description><identifier>ISSN: 0145-479X</identifier><identifier>EISSN: 1573-6881</identifier><identifier>DOI: 10.1023/A:1005532912212</identifier><identifier>PMID: 11768307</identifier><language>eng</language><publisher>United States: Springer Nature B.V</publisher><subject>Animals ; Catalysis ; Cations, Divalent ; Enzyme Inhibitors - pharmacology ; Enzymes ; Humans ; Kinetics ; Metals ; Nucleoside-Diphosphate Kinase - antagonists & inhibitors ; Nucleoside-Diphosphate Kinase - metabolism ; Nucleoside-Diphosphate Kinase - physiology ; Phosphorylation ; Proteins ; Substrate Specificity</subject><ispartof>Journal of bioenergetics and biomembranes, 2000-06, Vol.32 (3), p.237</ispartof><rights>Plenum Publishing Corporation 2000</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c280t-39ad6e9335954d9802845c85aeec920361ea9b8c5201ead6c0597c60bd7d2d533</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11768307$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lascu, I</creatorcontrib><creatorcontrib>Gonin, P</creatorcontrib><title>The catalytic mechanism of nucleoside diphosphate kinases</title><title>Journal of bioenergetics and biomembranes</title><addtitle>J Bioenerg Biomembr</addtitle><description>Nucleoside diphosphate kinases catalyze the reversible transfer of the gamma phosphate of nucleoside triphosphates to nucleoside diphosphates. This minireview presents recent advances in understanding the reaction mechanism using steady-state and fast kinetic studies, X-ray crystallography, and site-directed mutagenesis. We also briefly discuss the physiological relevance of in vitro studies.</description><subject>Animals</subject><subject>Catalysis</subject><subject>Cations, Divalent</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Enzymes</subject><subject>Humans</subject><subject>Kinetics</subject><subject>Metals</subject><subject>Nucleoside-Diphosphate Kinase - antagonists & inhibitors</subject><subject>Nucleoside-Diphosphate Kinase - metabolism</subject><subject>Nucleoside-Diphosphate Kinase - physiology</subject><subject>Phosphorylation</subject><subject>Proteins</subject><subject>Substrate Specificity</subject><issn>0145-479X</issn><issn>1573-6881</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><recordid>eNo1jztPwzAUhS0EoqEws6GIPXDtmxvbbFXFS6rEUiS2yLVvlZTmQZwM_fdUokznDJ--oyPErYQHCQofF08SgAiVlUpJdSYSSRqzwhh5LhKQOWW5tl8zcRXjDgAMEFyKmZS6MAg6EXZdcerd6PaHsfZpw75ybR2btNum7eT33MU6cBrqvupiX7mR0--6dZHjtbjYun3km1POxefL83r5lq0-Xt-Xi1XmlYExQ-tCwRaRLOXBGlAmJ2_IMXurAAvJzm6MJwXHFgoPZLUvYBN0UIEQ5-L-z9sP3c_EcSx33TS0x8lSk7E5ItgjdHeCpk3DoeyHunHDofw_ir8sw1PG</recordid><startdate>20000601</startdate><enddate>20000601</enddate><creator>Lascu, I</creator><creator>Gonin, P</creator><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>3V.</scope><scope>7QO</scope><scope>7QP</scope><scope>7TK</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>P64</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope></search><sort><creationdate>20000601</creationdate><title>The catalytic mechanism of nucleoside diphosphate kinases</title><author>Lascu, I ; Gonin, P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c280t-39ad6e9335954d9802845c85aeec920361ea9b8c5201ead6c0597c60bd7d2d533</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Animals</topic><topic>Catalysis</topic><topic>Cations, Divalent</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Enzymes</topic><topic>Humans</topic><topic>Kinetics</topic><topic>Metals</topic><topic>Nucleoside-Diphosphate Kinase - antagonists & inhibitors</topic><topic>Nucleoside-Diphosphate Kinase - metabolism</topic><topic>Nucleoside-Diphosphate Kinase - physiology</topic><topic>Phosphorylation</topic><topic>Proteins</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lascu, I</creatorcontrib><creatorcontrib>Gonin, P</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>ProQuest Central (Corporate)</collection><collection>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>ProQuest Health and Medical</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>AUTh Library subscriptions: ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection (Proquest) (PQ_SDU_P3)</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>ProQuest Science Journals</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Materials Science Collection</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><jtitle>Journal of bioenergetics and biomembranes</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lascu, I</au><au>Gonin, P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The catalytic mechanism of nucleoside diphosphate kinases</atitle><jtitle>Journal of bioenergetics and biomembranes</jtitle><addtitle>J Bioenerg Biomembr</addtitle><date>2000-06-01</date><risdate>2000</risdate><volume>32</volume><issue>3</issue><spage>237</spage><pages>237-</pages><issn>0145-479X</issn><eissn>1573-6881</eissn><abstract>Nucleoside diphosphate kinases catalyze the reversible transfer of the gamma phosphate of nucleoside triphosphates to nucleoside diphosphates. This minireview presents recent advances in understanding the reaction mechanism using steady-state and fast kinetic studies, X-ray crystallography, and site-directed mutagenesis. We also briefly discuss the physiological relevance of in vitro studies.</abstract><cop>United States</cop><pub>Springer Nature B.V</pub><pmid>11768307</pmid><doi>10.1023/A:1005532912212</doi></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0145-479X |
ispartof | Journal of bioenergetics and biomembranes, 2000-06, Vol.32 (3), p.237 |
issn | 0145-479X 1573-6881 |
language | eng |
recordid | cdi_proquest_journals_758943309 |
source | Springer Nature |
subjects | Animals Catalysis Cations, Divalent Enzyme Inhibitors - pharmacology Enzymes Humans Kinetics Metals Nucleoside-Diphosphate Kinase - antagonists & inhibitors Nucleoside-Diphosphate Kinase - metabolism Nucleoside-Diphosphate Kinase - physiology Phosphorylation Proteins Substrate Specificity |
title | The catalytic mechanism of nucleoside diphosphate kinases |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-01T17%3A48%3A00IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20catalytic%20mechanism%20of%20nucleoside%20diphosphate%20kinases&rft.jtitle=Journal%20of%20bioenergetics%20and%20biomembranes&rft.au=Lascu,%20I&rft.date=2000-06-01&rft.volume=32&rft.issue=3&rft.spage=237&rft.pages=237-&rft.issn=0145-479X&rft.eissn=1573-6881&rft_id=info:doi/10.1023/A:1005532912212&rft_dat=%3Cproquest_pubme%3E2166021341%3C/proquest_pubme%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c280t-39ad6e9335954d9802845c85aeec920361ea9b8c5201ead6c0597c60bd7d2d533%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=758943309&rft_id=info:pmid/11768307&rfr_iscdi=true |