WordNet

any of several complex proteins that are produced by cells and act as catalysts in specific biochemical reactions
the 5th letter of the Roman alphabet (同)e
causing motion or action or change (同)actuating

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1. 脊髄性筋萎縮症 spinal muscular atrophy
2. 陣痛誘発前に未成熟な頸管を熟化させる手技 techniques for ripening the unfavorable cervix prior to induction
3. 新生児におけるチアノーゼ性心疾患の診断および初期マネージメント diagnosis and initial management of cyanotic heart disease in the newborn
4. 敗血症を起こした幼児に対するアプローチ approach to the septic appearing infant
5. 下肢の慢性重症下肢虚血の治療 treatment of chronic lower extremity critical limb ischemia

English Journal

E1-catalyzed ubiquitin C-terminal amidation for the facile synthesis of deubiquitinase substrates.

Wang XA, Kurra Y, Huang Y, Lee YJ, Liu WR.Author information Department of Chemistry, Texas A&M University, College Station, TX 77843 (USA).AbstractWill Ub my partner? The ubiquitin (Ub)-activating enzyme (E1) was used to catalyze an amidation reaction to functionalize the C terminus of Ub with unique functional groups, such as thiol, azide, alkyne, and alkene groups, with high efficiency and yield (>90 %). These groups were then applied for the facile synthesis of fluorophore-conjugated ubiquitin and specifically conjugated diubiquitin substrates for deubiquitinases.
Chembiochem : a European journal of chemical biology.Chembiochem.2014 Jan 3;15(1):37-41. doi: 10.1002/cbic.201300608. Epub 2013 Dec 16.
Will Ub my partner The ubiquitin (Ub)-activating enzyme (E1) was used to catalyze an amidation reaction to functionalize the C terminus of Ub with unique functional groups, such as thiol, azide, alkyne, and alkene groups, with high efficiency and yield (>90 %). These groups were then applied f
PMID 24357003

NMR structural studies of the first catalytic half-domain of ubiquitin activating enzyme.

Jaremko M1, Jaremko L2, Nowakowski M3, Wojciechowski M4, Szczepanowski RH4, Panecka R4, Zhukov I5, Bochtler M6, Ejchart A7.Author information 1Max Planck Institute for Biophysical Chemistry, Department for NMR-based Structural Biology, Am Fassber 11, 37077 Göttingen, Germany.2Max Planck Institute for Biophysical Chemistry, Department for NMR-based Structural Biology, Am Fassber 11, 37077 Göttingen, Germany; Deutsches Zentrum für Neurodegenerative Erkrankungen (DZNE), Am Fassberg 11, 37077 Göttingen, Germany.3Faculty of Chemistry, Biological and Chemical Research Centre, University of Warsaw, Żwirki i Wigury 101, 02-089 Warsaw, Poland.4International Institute of Molecular and Cell Biology, Trojdena 4, 02-109 Warsaw, Poland.5Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5A, 02-106 Warsaw, Poland; NanoBioMedical Centre, Adam Mickiewicz University, Umultowska 85, 61-614 Poznan, Poland.6International Institute of Molecular and Cell Biology, Trojdena 4, 02-109 Warsaw, Poland; Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5A, 02-106 Warsaw, Poland.7Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5A, 02-106 Warsaw, Poland. Electronic address: aejchart@ibb.waw.pl.AbstractWe report a high resolution NMR structure and (15)N relaxation studies of the first catalytic cysteine half-domain (FCCH) of the mouse ubiquitin-activating enzyme E1, together with interaction studies of FCCH and the other catalytic E1 subdomain - SCCH (second catalytic cysteine half-domain). In solution, mouse FCCH forms a well-defined six-stranded antiparallel β-barrel structure, a common fold for many proteins with a variety of cellular functions. (15)N relaxation data reveal FCCH complex backbone dynamics and indicate which residues experience slow intramolecular motions. Some of these residues make contacts with the polar face of ubiquitin in the co-crystal structure of yeast E1 and ubiquitin. However, the titration of FCCH with ubiquitin does not show any visible chemical shift changes in the 2D (1)H/(15)N HSQC spectra of the FCCH. The 2D (1)H/(15)N HSQC experiments performed both for each catalytic half-domain individually and for their equimolar mixture in the milimolar concentration range display no detectable chemical shift perturbation, suggesting a lack of interaction between the two subdomains unless they are covalently linked via the adenylation domain.
Journal of structural biology.J Struct Biol.2014 Jan;185(1):69-78. doi: 10.1016/j.jsb.2013.10.020. Epub 2013 Nov 6.
We report a high resolution NMR structure and (15)N relaxation studies of the first catalytic cysteine half-domain (FCCH) of the mouse ubiquitin-activating enzyme E1, together with interaction studies of FCCH and the other catalytic E1 subdomain - SCCH (second catalytic cysteine half-domain). In sol
PMID 24211821

Cloning of ubiquitin-activating enzyme and ubiquitin-conjugating enzyme genes from Gracilaria lemaneiformis and their activity under heat shock.

Li GQ1, Zang XN2, Zhang XC1, Lu N1, Ding Y1, Gong L1, Chen WC1.Author information 1Key Laboratory of Marine Genetics and Breeding, Ministry of Education, Ocean University of China, Qingdao 266003, Shandong, China.2Key Laboratory of Marine Genetics and Breeding, Ministry of Education, Ocean University of China, Qingdao 266003, Shandong, China. Electronic address: xnzang@ouc.edu.cn.AbstractTo study the response of Gracilaria lemaneiformis to heat stress, two key enzymes - ubiquitin-activating enzyme (E1) and ubiquitin-conjugating enzyme (E2) - of the Ubiquitin/26S proteasome pathway (UPP) were studied in three strains of G. lemaneiformis-wild type, heat-tolerant cultivar 981 and heat-tolerant cultivar 07-2. The full length DNA sequence of E1 contained only one exon. The open reading frame (ORF) sequence was 981 nucleotides encoding 326 amino acids, which contained conserved ATP binding sites (LYDRQIRLWGLE, ELAKNVLLAGV, LKEMN, VVCAI) and the ubiquitin-activating domains (VVCAI…LMTEAC, VFLDLGDEYSYQ, AIVGGMWGRE). The gene sequence of E2 contained four exons and three introns. The sum of the four exons gave an open reading frame sequence of 444 nucleotides encoding 147 amino acids, which contained a conserved ubiquitin-activating domain (GSICLDIL), ubiquitin-conjugating domains (RIYHPNIN, KVLLSICSLL, DDPLV) and ubiquitin-ligase (E3) recognition sites (KRI, YPF, WSP). Real-time-PCR analysis of transcription levels of E1 and E2 under heat shock conditions (28°C and 32°C) showed that in wild type, transcriptions of E1 and E2 were up-regulated at 28°C, while at 32°C, transcriptions of the two enzymes were below the normal level. In cultivar 981 and cultivar 07-2 of G. lemaneiformis, the transcription levels of the two enzymes were up-regulated at 32°C, and transcription level of cultivar 07-2 was even higher than that of cultivar 981. These results suggest that the UPP plays an important role in high temperature resistance of G. lemaneiformis and the bioactivity of UPP is directly related to the heat-resistant ability of G. lemaneiformis.
Gene.Gene.2013 Dec 21. pii: S0378-1119(13)01678-8. doi: 10.1016/j.gene.2013.12.017. [Epub ahead of print]
To study the response of Gracilaria lemaneiformis to heat stress, two key enzymes - ubiquitin-activating enzyme (E1) and ubiquitin-conjugating enzyme (E2) - of the Ubiquitin/26S proteasome pathway (UPP) were studied in three strains of G. lemaneiformis-wild type, heat-tolerant cultivar 981 and heat-
PMID 24365593

Japanese Journal

Himeic Acids E–G, New 4-Pyridone Derivatives from a Culture of Aspergillus sp.

Kuwana Toshiyuki,Miyazaki Mitsue,Kato Hikaru [他],Tsukamoto Sachiko
Chemical and Pharmaceutical Bulletin 61(1), 105-107, 2013
… Although himeic acid A inhibited the activity of ubiquitin-activating enzyme (E1), the three new derivatives did not. …
NAID 130003360720

Identification and Characterization of Feline UBE1L Gene

SHIMODE Sayumi,MIYAZAWA Takayuki,KOBAYASHI Takeshi,SATO Hisaaki,TANABE Taishi
Journal of Veterinary Medical Science 74(2), 235-239, 2012
… Addition of ISG15 known as ISGylation is an ubiquitin-like posttranslational modification. … Coexpression of ISG15 and ubiquitin-activating enzyme E1-like protein (UBE1L) is required to induce ISGylation. …
NAID 130001033063

創薬を指向した天然薬物学研究

塚本佐知子
YAKUGAKU ZASSHI 130(10), 1273-1281, 2010
… The ubiquitin-proteasome system (UPS) plays a major role in selective protein degradation and regulates various cellular events. …
NAID 130000451669