Dinamin

Dinamin GTPaza
Identifikatori
EC broj 3.6.5.5
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB RCSB PDB PDBe PDBj PDBsum
Pretraga
PMC articles
PubMed articles
NCBI Protein search
Dinamin N
Struktura beznukleotidnog miozinskog motornog domena II iz Dictyostelium discoideum spojena sa GTPaznim domenom dinamina 1 iz Rattus norvegicus
Identifikatori
Simbol Dynamin_N
Pfam PF00350
Pfam klan CL0023
InterPro IPR001401
PROSITE PDOC00362
Centralni region dinamina
Struktura beznukleotidnog miozinskog motornog domena II iz Dictyostelium discoideum spojena sa GTPaznim domenom dinamina 1 iz Rattus norvegicus
Identifikatori
Simbol Dynamin_M
Pfam PF01031
InterPro IPR000375

Dinamin je GTPaza odgovorna za endocitozu u eukariotskim ćelijama. Dinamini prvenstveno učestvuju u odvajanju novoformiranih vezikula od membrane jednog ćelijskog kompartmana, i njihovom usmeravanju i spajanju sa drugim kompartmanom. Oni posreduju endocitozu sa ćelijske površine (posebno internalizaciju kaveola), kao i sa Goldžijevog aprata.[1][2][3] Dinamin učestvuje i nizu procesa deobe organela,[4] citokineze i u pružanju otpora mikrobnim patogenim.

Dinamin pripada dinaminskoj superfamiliji koja obuhvata klasične dinamine, dinaminu slične proteine, Mx proteine, OPA, mitofuzine, i GBP proteine.

Dinamin je enzim sa 96 kDa. On je privi put izolovan tokom pokušaja da se izoluju motori bazirani na mikrotubulama iz goveđeg mozga. Dinamin je intenzivno proučavan u kontekstu pupljenja klatrinom pokrivenih vezikula sa ćelijske membrane.[3][5]

Reference

  1. Henley, J.R., Cao, H., McNicven, M.A. (1999). “Participation of dynamin in the biogenesis of cytoplasmic vesicles”. The FASEB Journal, 13, S243-S247.
  2. Hinshaw, J. “Dynamin overview: The Role of Dynamin in Membrane Fission”. Arhivirano 2011-10-15 na Wayback Machine-u National institute of diabetes & digestive & kidney diseases, Laboratory of cell biochemistry and biology. accessed 021806.
  3. 3,0 3,1 Urrutia R., Henley J.R., Cook T., McNiven M.A. (1997). „The dynamins: Redundant or distinct functions for an expanding family of related GTPases?”. Proc. Natl Acad. Sci. USA 94 (2): 377–384. DOI:10.1073/pnas.94.2.377. 
  4. Thoms S, Erdmann R (Oct 2005). „Dynamin-related proteins and Pex11 proteins in peroxisome division and proliferation.”. FEBS J 272 (20): 5169–81. DOI:10.1111/j.1742-4658.2005.04939.x. PMID 16218949. 
  5. McMahon. (2004). “Researching Endocytic Mechanisms: Dynamin:. Arhivirano 2012-03-05 na Wayback Machine-u Accompaniment of Nature Reviews on Molecular Cell Biology, 5, 133-147.

Literatura

  • Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X. 
  • Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036. 
  • Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0. 
  • Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097. 
  • Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X. 
  • Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842. 

Spoljašnje veze

Dinamin na Wikimedijinoj ostavi
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3.6.1
Pirofosfataza (Neorganska, Tiamin Apiraza  Tiamin trifosfataza
3.6.23.6.3-4: ATPaza
3.6.3
Cu++ (3.6.3.4)
Menkes/ATP7A  Vilson/ATP7B
Ca+ (3.6.3.8)
SERCA (ATP2A1, ATP2A2, ATP2A3)  Membrana plazme (ATP2B1, ATP2B2, ATP2B3, ATP2B4)  SPCA (ATP2C1, ATP2C2)
Na+/K+ (3.6.3.9)
ATP1A1  ATP1A2  ATP1A3  ATP1A4  ATP1B1  ATP1B2  ATP1B3  ATP1B4
H+/K+ (3.6.3.10)
ATP4A
Druge P-tip ATPaze
ATP8B1  ATP10A  ATP11B  ATP12A  ATP13A2  ATP13A3 
3.6.4
Dinein  Kinezin  Miozin
3.6.5: GTPaze
Gαs  Gαi (GNAI1, GNAI2, GNAI3 Gαq/11 (GNAQ, GNA11 Gα12/13 (GNA12, GNA13 Transducin (GNAT1, GNAT2)
Ras  Rab (Rab27)  Arf (Arf6)  Ran  Rheb  Ro familija (RhoA, RhoB, CDC42, Rac1)  Rap
3.6.5.3: Protein-sintetišuće GTPaze
Prokariotski (IF-2, EF-Tu, EF-G Eukariotski
3.6.5.5-6: Polimerizacioni motori
Dinamin  Tubulin
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
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Teme
Tipovi
EC1 Oksidoreduktaze/spisak  • EC2 Transferaze/spisak  • EC3 Hidrolaze/spisak  • EC4 Lijaze/spisak  • EC5 Izomeraze/spisak  • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6