| pubmed-article:12146964 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12146964 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
| pubmed-article:12146964 | lifeskim:mentions | umls-concept:C0024660 | lld:lifeskim |
| pubmed-article:12146964 | lifeskim:mentions | umls-concept:C0033640 | lld:lifeskim |
| pubmed-article:12146964 | lifeskim:mentions | umls-concept:C0233820 | lld:lifeskim |
| pubmed-article:12146964 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
| pubmed-article:12146964 | lifeskim:mentions | umls-concept:C0598002 | lld:lifeskim |
| pubmed-article:12146964 | pubmed:issue | 31 | lld:pubmed |
| pubmed-article:12146964 | pubmed:dateCreated | 2002-7-30 | lld:pubmed |
| pubmed-article:12146964 | pubmed:abstractText | The SRPK family is distinguished from typical eukaryotic protein kinases by several unique structural features recently elucidated by X-ray diffraction methods [Nolen et al. (2001) Nat. Struct. Biol. 8, 176-183]. To determine whether these features impart unique catalytic function, the phosphorylation of the physiological Sky1p substrate, Npl3p, was monitored using steady-state and pre-steady-state kinetic techniques. While Sky1p has a low apparent affinity for ATP compared to other protein kinases, it binds Npl3p with very high affinity. The latter is achieved through a combination of local and distal factors in the protein substrate. The phosphoryl donor ATP has access to the nucleotide pocket in the absence or presence of Npl3p, indicating that a large protein substrate does not enforce an ordered addition of ligands. Sky1p binds two Mg(2+)-the first is essential whereas the second further enhances catalysis. While the turnover number is low (0.5 s(-1)), Npl3p is rapidly phosphorylated in the active site (40 s(-1)) based on single turnover experiments. These results indicate that Sky1p employs a catalytic pathway involving fast phosphoryl transfer followed by slow net release of products. These studies represent the first kinetic investigation of a member of the SRPK family and the first pre-steady-state kinetic study of a protein kinase using a natural protein substrate. | lld:pubmed |
| pubmed-article:12146964 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12146964 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12146964 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12146964 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12146964 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12146964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12146964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12146964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12146964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12146964 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12146964 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:12146964 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:12146964 | pubmed:author | pubmed-author:CamSS | lld:pubmed |
| pubmed-article:12146964 | pubmed:author | pubmed-author:GhoshGourisan... | lld:pubmed |
| pubmed-article:12146964 | pubmed:author | pubmed-author:AubolBrandon... | lld:pubmed |
| pubmed-article:12146964 | pubmed:author | pubmed-author:NolenBradB | lld:pubmed |
| pubmed-article:12146964 | pubmed:author | pubmed-author:AdamsJoseph... | lld:pubmed |
| pubmed-article:12146964 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12146964 | pubmed:day | 6 | lld:pubmed |
| pubmed-article:12146964 | pubmed:volume | 41 | lld:pubmed |
| pubmed-article:12146964 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12146964 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12146964 | pubmed:pagination | 10002-9 | lld:pubmed |
| pubmed-article:12146964 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:12146964 | pubmed:meshHeading | pubmed-meshheading:12146964... | lld:pubmed |
| pubmed-article:12146964 | pubmed:meshHeading | pubmed-meshheading:12146964... | lld:pubmed |
| pubmed-article:12146964 | pubmed:meshHeading | pubmed-meshheading:12146964... | lld:pubmed |
| pubmed-article:12146964 | pubmed:meshHeading | pubmed-meshheading:12146964... | lld:pubmed |
| pubmed-article:12146964 | pubmed:meshHeading | pubmed-meshheading:12146964... | lld:pubmed |
| pubmed-article:12146964 | pubmed:meshHeading | pubmed-meshheading:12146964... | lld:pubmed |
| pubmed-article:12146964 | pubmed:meshHeading | pubmed-meshheading:12146964... | lld:pubmed |
| pubmed-article:12146964 | pubmed:meshHeading | pubmed-meshheading:12146964... | lld:pubmed |
| pubmed-article:12146964 | pubmed:meshHeading | pubmed-meshheading:12146964... | lld:pubmed |
| pubmed-article:12146964 | pubmed:meshHeading | pubmed-meshheading:12146964... | lld:pubmed |
| pubmed-article:12146964 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12146964 | pubmed:articleTitle | Mechanistic insights into Sky1p, a yeast homologue of the mammalian SR protein kinases. | lld:pubmed |
| pubmed-article:12146964 | pubmed:affiliation | Department of Chemistry and Biochemistry, University of California-San Diego, La Jolla, CA 92093, USA. | lld:pubmed |
| pubmed-article:12146964 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12146964 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12146964 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:12146964 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12146964 | lld:pubmed |
