Pseudolizin

Pseudolizin
Identifikatori
EC broj3.4.24.26
CAS broj171715-23-4
Baze podataka
IntEnzIntEnz pregled
BRENDABRENDA pristup
ExPASyNiceZyme pregled
KEGGKEGG pristup
MetaCycmetabolički put
PRIAMprofil
Strukture PBPRCSB PDB PDBe PDBj PDBsum
Pretraga
PMCčlanci
PubMedčlanci
NCBIproteini

Pseudolizin (EC 3.4.24.26, Pseudomonas elastaza, Pseudomonas aeruginosa neutralna metaloproteinaza) je enzim.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju

Hidroliza proteina uključujući elastin, kolagen tipa III i IV, fibronektin i imunoglobulin A, generalno sa glomaznim hidrofobnim grupama u P1'. Lanac insulina B se razlaže na identičnom šablonu prepoznavanja sa termolizinom, ali postoje razlike u specifinosti u drugim pogledima

Ovaj enzim pripada peptidaznoj familiji M4 (termolizinskoj familiji).

Reference

  1. ^ Morihara, K. & Tsuzuki, H. (1975). „Pseudomonas aeruginosa elastase: affinity chromatography and some properties as a metallo-neutral proteinase”. Agric. Biol. Chem. 39: 1123—1128. 
  2. ^ Nishino, N. & Powers, J.C. (1980). „Pseudomonas aeruginosa elastase. Development of a new substrate, inhibitors, and an affinity ligand”. J. Biol. Chem. 255: 3482—3486. PMID 6767718. 
  3. ^ Dreyfus, L.A. & Iglewski, B.H. (1986). „Purification and characterization of an extracellular protease of Legionella pneumophila”. Infect. Immun. 70: 736—743. PMID 3512431. 
  4. ^ Bever, R.A. & Iglewski, B.H. (1988). „Molecular characterization and nucleotide sequence of the Pseudomonas aeruginosa elastase structural gene”. J. Bacteriol. 170: 4309—4314. PMID 2842313. 
  5. ^ Black, W.J., Quinn, F.D. and Tompkins, L.S. (1990). „Legionella pneumophila zinc metalloprotease is structurally and functionally homologous to Pseudomonas aeruginosa elastase”. J. Bacteriol. 172: 2608—2613. PMID 2110146. CS1 одржавање: Вишеструка имена: списак аутора (веза)

Literatura

  • Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X. 
  • Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). 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 изд.). Wiley Classics Library. ISBN 0471303097. 
  • William P. Jencks (1987). Catalysis in Chemistry and Enzymology. Dover Publications. ISBN 0486654605. 

Spoljašnje veze

  • Pseudolysin на US National Library of Medicine Medical Subject Headings (MeSH)
  • п
  • р
  • у
3.4.11-19: Egzopeptidaza
3.4.11
Aminopeptidaza (Alanin, Arginil, Aspartil, Cistinil, Leucil, Glutamil, Metionil (1, 2), O)
3.4.13
Dipeptidaza (1, 2, 3)
3.4.14
Dipeptidil peptidaza (Katepsin C, Dipeptidil peptidaza-4) · Tripeptidil peptidaza (Tripeptidil peptidaza I, Tripeptidil peptidaza II)
3.4.15
3.4.16
Karboksipeptidaze serinskog tipa: Katepsin A · DD-transpeptidaza
3.4.17
Metalokarboksipeptidaze: Karboksipeptidaza (A, A2, B, C, E, Glutamat II)
Drugi/negrupisni
Metaloeksopeptidaza
3.4.21-24: Endopeptidaza3.4.99: Nepoznato
Stafilokinaza
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
  • п
  • р
  • у
Teme
Tipovi
  • 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
Portali:
  •  Molekularna i ćelijska biologija
  •  Hemija