ADP-ribosilhidrolase

ADP-ribosilhidrolase
struktur kristal ribosilglikohidrolase mj1187 dari Methanococcus jannaschii
Identifikasi
SimbolARH
PfamPF03747
InterProIPR005502
SCOP1t5j
SUPERFAMILY1t5j

Dalam biologi molekuler, keluarga (ADP-ribosil)hidrolase (ARH) mengandung enzim yang mengkatalisis hidrolisis modifikasi ADP-ribosil dari protein, asam nukleat, dan molekul kecil.[1]

Jenis

Keluarga ini memiliki tiga anggota pada manusia (ARH1-3): ARH1, yang juga disebut [Protein ADP-ribosylarginine] hidrolase, membelah ADP-ribosa-L-arginin,[2] ARH2, yang diprediksi tidak aktif secara enzimatik,[3] dan ARH3, yang terutama membelah ADP-ribosa-L-serin, tetapi juga terbukti menghidrolisis poli(ADP-ribosa), 1''-O-asetil-ADP-ribosa, dan alfa-nikotinamida adenina dinukleotida.[4][5][6][7] Keluarga ini juga mencakup ADP-ribosyl-(dinitrogen reductase) hydrolase (DraG) yang diketahui meregulasi dinitrogenase reduktase, enzim kunci dari jalur fiksasi nitrogen pada bakteri,[8][1] dan yang paling mengejutkan adalah kristalin ubur-ubur,[8][9] meskipun protein yang terakhir ini tampaknya telah kehilangan residu pada situs aktif yang diperkirakan.

Kelas Spesies Lokasi
intraseluler 		Aktivitas Fungsi
Bakteri Manusia Lainnya
I ARH1 retikulum endoplasma, sitoplasma ADP-ribosilarginin hidrolase inflamasi, stabilitas genom
II ARH2 sitoplasma, sarkomer jantung tidak aktif pertumbuhan ruang jantung
III ARH3 Nukleus, sitoplasma ADP-ribosilserin hidrolase perbaikan DNA
IV Kristalin J1[9] dan SelJ[10] tidak aktif Kristalin
V DraG ADP-ribosilarginin hidrolase Regulasi fiksasi nitrogen

Lihat pula

Referensi

  1. ^ a b Rack JG, Palazzo L, Ahel I (March 2020). "(ADP-ribosyl)hydrolases: structure, function, and biology". Genes & Development. 34 (5–6): 263–284. doi:10.1101/gad.334631.119. PMC 7050489. PMID 32029451.
  2. ^ Takada T, Iida K, Moss J (August 1993). "Cloning and site-directed mutagenesis of human ADP-ribosylarginine hydrolase". The Journal of Biological Chemistry. 268 (24): 17837–43. doi:10.1016/S0021-9258(17)46780-9. PMID 8349667.
  3. ^ Smith SJ, Towers N, Saldanha JW, Shang CA, Mahmood SR, Taylor WR, Mohun TJ (August 2016). "The cardiac-restricted protein ADP-ribosylhydrolase-like 1 is essential for heart chamber outgrowth and acts on muscle actin filament assembly". Developmental Biology. 416 (2): 373–88. doi:10.1016/j.ydbio.2016.05.006. PMC 4990356. PMID 27217161.
  4. ^ Fontana P, Bonfiglio JJ, Palazzo L, Bartlett E, Matic I, Ahel I (June 2017). "Serine ADP-ribosylation reversal by the hydrolase ARH3". eLife. 6 e28533. doi:10.7554/eLife.28533. PMC 5552275. PMID 28650317.
  5. ^ Stevens LA, Kato J, Kasamatsu A, Oda H, Lee DY, Moss J (December 2019). "The ARH and Macrodomain Families of α-ADP-ribose-acceptor Hydrolases Catalyze α-NAD + Hydrolysis". ACS Chemical Biology. 14 (12): 2576–2584. doi:10.1021/acschembio.9b00429. PMC 8388552. PMID 31599159.
  6. ^ Ono T, Kasamatsu A, Oka S, Moss J (November 2006). "The 39-kDa poly(ADP-ribose) glycohydrolase ARH3 hydrolyzes O-acetyl-ADP-ribose, a product of the Sir2 family of acetyl-histone deacetylases". Proceedings of the National Academy of Sciences of the United States of America. 103 (45): 16687–91. Bibcode:2006PNAS..10316687O. doi:10.1073/pnas.0607911103. PMC 1636516. PMID 17075046.
  7. ^ Oka S, Kato J, Moss J (January 2006). "Identification and characterization of a mammalian 39-kDa poly(ADP-ribose) glycohydrolase". The Journal of Biological Chemistry. 281 (2): 705–13. doi:10.1074/jbc.M510290200. PMID 16278211. S2CID 19256217.
  8. ^ a b Fitzmaurice WP, Saari LL, Lowery RG, Ludden PW, Roberts GP (August 1989). "Genes coding for the reversible ADP-ribosylation system of dinitrogenase reductase from Rhodospirillum rubrum". Molecular & General Genetics. 218 (2): 340–7. doi:10.1007/BF00331287. PMID 2506427. S2CID 35664554.
  9. ^ a b Piatigorsky J, Horwitz J, Norman BL (June 1993). "J1-crystallins of the cubomedusan jellyfish lens constitute a novel family encoded in at least three intronless genes". The Journal of Biological Chemistry. 268 (16): 11894–901. doi:10.1016/S0021-9258(19)50284-8. PMID 8505315.
  10. ^ Castellano S, Lobanov AV, Chapple C, Novoselov SV, Albrecht M, Hua D, et al. (November 2005). "Diversity and functional plasticity of eukaryotic selenoproteins: identification and characterization of the SelJ family". Proceedings of the National Academy of Sciences of the United States of America. 102 (45): 16188–93. doi:10.1073/pnas.0505146102. PMC 1283428. PMID 16260744.

Templat:InterPro content

Ikon rintisan

Artikel bertopik enzim ini adalah sebuah rintisan. Anda dapat membantu Wikipedia dengan mengembangkannya.

Content Disclaimer

Informasi ini disarikan dari Wikipedia dan disajikan kembali untuk tujuan edukasi. Konten tersedia di bawah lisensi CC BY-SA 3.0. Kami tidak bertanggung jawab atas ketidakakuratan data yang bersumber dari kontribusi publik tersebut.

  1. The information displayed on this website is sourced in part or in whole from Wikipedia and has been adapted for the purpose of restating it. We strive to provide accurate and relevant information, however:
  2. There is no guarantee of absolute accuracy. Wikipedia is an open, collaborative project that can be edited by anyone, so information is subject to change.
  3. It is not intended to constitute professional advice. The content displayed is for informational and educational purposes only. For important decisions (e.g., medical, legal, or financial), please consult a professional.
  4. Content copyright. Wikipedia is licensed under the Creative Commons Attribution-ShareAlike License (CC BY-SA). This means that content may be reused with appropriate attribution and shared under a similar license.
  5. Responsible use. Any risk arising from the use of information from this website is entirely the responsibility of the user.
Kembali kehalaman sebelumnya