aceE - pyruvate dehydrogenase E1 component-BMKCloudï½ç¾è¿å®¢äº

例如："NBL1", "4681", "drought"

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944834 aceE

基因描述

Type	Description
Definition	pyruvate dehydrogenase E1 component

研究结论

Date	Results	Publications
2014-10-11 10:10:00	The inclusion of each additional domain of E2p strengthened the interaction with E1p, and the interaction was strongest with intact E2p.	24742683
2010-05-10 11:16:00	thiamin cofactor communication in the Escherichia coli pyruvate dehydrogenase complex E1 component active centers is a "direct pathway" between the 4'-aminopyrimidine N1' atoms	20106967
2010-01-25 12:01:00	Observations suggest a mode of cooperativity in the E1 component that is consistent with the dynamical hypothesis shown to satisfactorily explain cooperativity in many well studied enzymes.	19801660
2010-01-21 00:00:00	crystal structure	16531404
2010-01-21 00:00:00	the dynamic loop at the active center of the Escherichia coli pyruvate dehydrogenase complex E1 component modulates substrate utilization and chemical communication with the E2 component	17635929

名称对应

Type	IDs
Synonymous	ECK0113
Gene	UniProtKB-ID: ODP1_ECOLI UniprotKB: P0AFG8 UniParc: UPI00000480B7 EMBL: AP009048, V01498, U00096, S67363 EnsemblGenome: BAB96684, b0114 KO: ecj:JW0110, eco:b0114
Nucleutide sequences	EMBL-CDS: AAB29357.1, CAA24740.1, BAB96684.2, AAC73225.1 EnsemblGenome_TRS: AAC73225, BAB96684
Protein sequencees	EnsemblGenome_PRO: AAC73225, BAB96684 RefSeq: NP_414656.1
Others	UniRef100: UniRef100_P0AFG9 UniRef90: UniRef90_P0AFG9 UniRef50: UniRef50_P0AFG9

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mRNA

Protein

UniprotKB

Description

Refseq

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Location

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Pubmed编号	文献信息	发表日期	相关基因
24742683	Structure and function of the catalytic domain of the dihydrolipoyl acetyltransferase component in Escherichia coli pyruvate dehydrogenase complex. J Biol Chem Junjie Wang , Natalia S Nemeria , Krishnamoorthy Chandrasekhar , Sowmini Kumaran , Palaniappa Arjunan , Shelley Reynolds , Guillermo Calero , Roman Brukh , Lazaros Kakalis , William Furey , Frank Jordan	2014-05-30	-
22157000	YajL, prokaryotic homolog of parkinsonism-associated protein DJ-1, functions as a covalent chaperone for thiol proteome. J Biol Chem Hai-Tuong Le , ValÃ©rie Gautier , Fatoum Kthiri , Abderrahim Malki , Nadia Messaoudi , Mouadh Mihoub , Ahmed Landoulsi , Young Jun An , Sun-Shin Cha , Gilbert Richarme	2012-02-17	-
20106967	Communication between thiamin cofactors in the Escherichia coli pyruvate dehydrogenase complex E1 component active centers: evidence for a "direct pathway" between the 4'-aminopyrimidine N1' atoms. J Biol Chem Natalia S Nemeria , Palaniappa Arjunan , Krishnamoorthy Chandrasekhar , Madouna Mossad , Kai Tittmann , William Furey , Frank Jordan	2010-04-09	-
19801660	Conformational ensemble modulates cooperativity in the rate-determining catalytic step in the E1 component of the Escherichia coli pyruvate dehydrogenase multienzyme complex. J Biol Chem Sachin Kale , Frank Jordan	2009-11-27	-
19679089	A surface loop directs conformational switching of a lipoyl domain between a folded and a novel misfolded structure. Structure Katherine M Stott , Adlina M Yusof , Richard N Perham , D Dafydd Jones	2009-08-12	-
18216265	Efficient coupling of catalysis and dynamics in the E1 component of Escherichia coli pyruvate dehydrogenase multienzyme complex. Proc. Natl. Acad. Sci. U.S.A. Sachin Kale , GÃ¶zde Ulas , Jaeyoung Song , Gary W Brudvig , William Furey , Frank Jordan	2008-01-29	aceE
17635929	A dynamic loop at the active center of the Escherichia coli pyruvate dehydrogenase complex E1 component modulates substrate utilization and chemical communication with the E2 component. J Biol Chem Sachin Kale , Palaniappa Arjunan , William Furey , Frank Jordan	2007-09-21	-
17182735	The 1',4'-iminopyrimidine tautomer of thiamin diphosphate is poised for catalysis in asymmetric active centers on enzymes. Proc. Natl. Acad. Sci. U.S.A. Natalia Nemeria , Sumit Chakraborty , Ahmet Baykal , Lioubov G Korotchkina , Mulchand S Patel , Frank Jordan	2007-01-02	aceE
17187058	Absolute protein expression profiling estimates the relative contributions of transcriptional and translational regulation. Nat. Biotechnol. Peng Lu , Christine Vogel , Rong Wang , Xin Yao , Edward M Marcotte	2007-01-01	sspA, talB, dnaK, dnaJ, rpsT, ileS, dapB, carB, ftsZ, murE, aceF, acpP, surA, secA, can, aceE, panB, argF, lpxA, dksA, lpd, erpA, skp, dapD, acnB, tsf, glnH, fabZ, metQ, accA, galM, sodB, panC, pyrH, codA, opgG, pepD, tauB, eno, proC, phoR, thiI, gpmA, leuC, tig, clpP, clpX, lon, adk, htpG, acrB, trpD, apt, ydgH, rplT, purK, ompT, thrC, ybeD, ahpC, purR, glf, serA, miaB, pgm, seqA, rfbB, iscR, asnB, mprA, fldA, fur, sucA, sucB, hisJ, glnS, sucC, sucD, gltA, bioB, pheT, bioD, metK, sdhA, ybiC, tolB, ybiT, ldtB, moeA, gsiB, yliE, ihfA, serS, pflB, serC, aroA, ihfB, rpsA, mukE
17070897	Acetylphosphinate is the most potent mechanism-based substrate-like inhibitor of both the human and Escherichia coli pyruvate dehydrogenase components of the pyruvate dehydrogenase complex. Bioorg. Chem. Natalia S Nemeria , Lioubov G Korotchkina , Sumit Chakraborty , Mulchand S Patel , Frank Jordan	2006-12-01	aceF, aceE

研究热度

热点单位

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热点人员

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