アデニリルトランスフェラーゼ、アデニル酸転移酵素
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2015/08/13 23:42:03」(JST)
[Wiki en表示]
Molybdopterin-synthase adenylyltransferase |
Identifiers |
EC number |
2.7.7.80 |
Databases |
IntEnz |
IntEnz view |
BRENDA |
BRENDA entry |
ExPASy |
NiceZyme view |
KEGG |
KEGG entry |
MetaCyc |
metabolic pathway |
PRIAM |
profile |
PDB structures |
RCSB PDB PDBe PDBsum |
Search |
PMC |
articles |
PubMed |
articles |
NCBI |
proteins |
|
Molybdopterin-synthase adenylyltransferase (EC 2.7.7.80, MoeB, adenylyltransferase and sulfurtransferase MOCS3) is an enzyme with system name ATP:molybdopterin-synthase adenylyltransferase.[1][2] This enzyme catalyses the following chemical reaction
- ATP + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly diphosphate + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP
This enzyme adenylates the C-terminus of the small subunit of the molybdopterin synthase.
References
- ^ Leimkuhler, S., Wuebbens, M.M. and Rajagopalan, K.V. (2001). "Characterization of Escherichia coli MoeB and its involvement in the activation of molybdopterin synthase for the biosynthesis of the molybdenum cofactor". J. Biol. Chem. 276 (37): 34695–34701. doi:10.1074/jbc.M102787200. PMID 11463785.
- ^ Matthies, A., Nimtz, M. and Leimkuhler, S. (2005). "Molybdenum cofactor biosynthesis in humans: identification of a persulfide group in the rhodanese-like domain of MOCS3 by mass spectrometry". Biochemistry 44: 7912–7920. doi:10.1021/bi0503448. PMID 15910006.
External links
- Molybdopterin-synthase adenylyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH)
UpToDate Contents
全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.
English Journal
- Identification of genes involved in rice seed priming in the early imbibition stage.
- Cheng J1, Wang L1, Zeng P1, He Y1, Zhou R1, Zhang H1, Wang Z1.
- Plant biology (Stuttgart, Germany).Plant Biol (Stuttg).2016 Feb 2. doi: 10.1111/plb.12438. [Epub ahead of print]
- Phase II of seed imbibition is a critical process during seed priming. To identify genes involved in rice seed priming, the altered proteins between the dry and imbibed (24 h) seeds were compared using a two-dimensional gel electrophoresis system in this stuy. Ten significantly changed proteins (fol
- PMID 26833720
- Structural insights into the synthesis of FMN in prokaryotic organisms.
- Herguedas B1, Lans I1, Sebastián M1, Hermoso JA2, Martínez-Júlvez M1, Medina M1.
- Acta crystallographica. Section D, Biological crystallography.Acta Crystallogr D Biol Crystallogr.2015 Dec 1;71(Pt 12):2526-42. doi: 10.1107/S1399004715019641. Epub 2015 Nov 27.
- Riboflavin kinases (RFKs) catalyse the phosphorylation of riboflavin to produce FMN. In most bacteria this activity is catalysed by the C-terminal module of a bifunctional enzyme, FAD synthetase (FADS), which also catalyses the transformation of FMN into FAD through its N-terminal FMN adenylyltransf
- PMID 26627660
- Clinical and genetic findings in a family with NMNAT1-associated Leber congenital amaurosis: case report and review of the literature.
- Hedergott A1, Volk AE2,3, Herkenrath P4, Thiele H5, Fricke J6, Altmüller J5,7, Nürnberg P5,8,9, Kubisch C2,3, Neugebauer A6.
- Graefe's archive for clinical and experimental ophthalmology = Albrecht von Graefes Archiv für klinische und experimentelle Ophthalmologie.Graefes Arch Clin Exp Ophthalmol.2015 Dec;253(12):2239-46. doi: 10.1007/s00417-015-3174-0. Epub 2015 Oct 13.
- BACKGROUND: Leber congenital amaurosis (LCA) is a severe retinal dystrophy, typically manifesting in the first year of life. Mutations in more than 18 genes have been reported to date. In recent studies, biallelic mutations in NMNAT1 encoding nicotinamide mononucleotide adenylyltransferase 1 have be
- PMID 26464178
Japanese Journal
- Protection of vincristine-induced neuropathy by WldS expression and the independence of the activity of Nmnat1
- Watanabe Masashi,Tsukiyama Tadasuke,Hatakeyama Shigetsugu
- Neuroscience Letters 411(3), 228-232, 2007-01-16
- … The slow Wallerian degeneration protein (WldS), a fusion protein containing amino-terminal E4B and full-length nicotinamide mononucleotide adenylyltransferase 1 (Nmnat1), delays axon degeneration caused by physical damages, toxins and genetic mutations which result in patients being diagnosed with neurodegenerative diseases. …
- NAID 120000969949
- A nicotinamide mononucleotide adenylyltransferase with unique adenylyl group donor specificity from a hyperthermophilic archaeon, Pyrococcus horikoshii OT-3
- Sakuraba H,Kanai K,Goda S,Kawarabayasi Y,Ohshima T
- JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC 23(2-6), 273-279, 2003
- NAID 120004253652
Related Links
- Definition of Adenylyltransferase with photos and pictures, translations, sample usage, and additional links for more information. ... ¹ Source: wiktionary.com Adenylyltransferase Pictures Click the following link to bring up a new ...
- For Reference Purpose Only! NMNAT2 (Nicotinamide mononucleotide adenylyltransferase 2) Product Data Sheet For Research Use Only, Not for use in diagnostic procedures Cat#: CY-E1252-2 1 Version#: 120420 NMNAT2
Related Pictures
★リンクテーブル★
[★]
- 英
- adenylyltransferase
- 関
- アデニリルトランスフェラーゼ
[★]
ニコチンアミドヌクレオチドアデニル基転移酵素、ニコチンアミドヌクレオチドアデニリルトランスフェラーゼ
[★]
硫酸アデニルトランスフェラーゼ、硫酸アデニリルトランスフェラーゼ
- 関
- ATP sulfurylase、sulfurylase
[★]
グルコース-1-リン酸アデニリルトランスフェラーゼ
- 関
- ADP-glucose pyrophosphorylase
[★]
ポリヌクレオチドアデニリルトランスフェラーゼ
- 関
- poly A polymerase