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Endo-1,3(4)-b-glukanaza
Identifikatori
EC broj	3.2.1.6
CAS broj	62213-14-3
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

Endo-1,3(4)-b-glukanaza (EC 3.2.1.6, endo-1,3-beta-D-glukanaza, laminaranaza, beta-1,3-glukanaza, beta-1,3-1,4-glukanaza, endo-1,3-beta-glukanaza, endo-beta-1,3(4)-glukanaza, endo-beta-1,3-1,4-glukanaza, endo-beta-(1->3)-D-glukanaza, endo-1,3-1,4-beta-D-glukanaza, endo-beta-(1-3)-D-glukanaza, endo-beta-1,3-glukanaza IV, endo-1,3-beta-D-glukanaza, 1,3-(1,3, 1,4)-beta-D-glukan 3(4)-glukanohidrolaza) je enzim sa sistematskim imenom 3(or 4)-beta-D-glukan 3(4)-glukanohidrolaza.^[1]^[2]^[3]^[4]^[5] Ovaj enzim katalizuje sledeću hemijsku reakciju

Endohidroliza (1->3)- ili (1->4)-veza u beta-D-glukanima, gde je glukozni ostatak hidrolizovane veze supstituisan na C-3

Supstrati su laminarin, lihenin i D-glukani iz žitarica.

Reference

↑ Barras, D.R. and Stone, B.A. (1969). „β-1,3-Glucan hydrolases from Euglena gracilis. I. The nature of the hydrolases”. Biochim. Biophys. Acta 191: 329-341. PMID 5354264.
↑ Barras, D.R. and Stone, B.A. (1969). „β-1,3-Glucan hydrolases from Euglena gracilis. II. Purification and properties of the β-1,3-glucan exo-hydrolase”. Biochim. Biophys. Acta 191: 342-353. PMID 5354265.
↑ Cunningham, L.W. and Manners, D.J. (1961). „Enzymic degradation of lichenin”. Biochem. J. 80: 42-42.
↑ Reese, E.T. and Mandels, M. (1959). „β-D-1,3-Glucanases in fungi”. Can. J. Microbiol. 5: 173-185. PMID 13638895.
↑ Sova, V.V., Elyakova, L.A. and Vaskovsky, V.E. (1970). „Purification and some properties of β-1,3-glucan glucanohydrolase from the crystalline style of bivalvia, Spisula sachalinensis”. Biochim. Biophys. Acta 212: 111-115. PMID 5500926.

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.

Vanjske veze

MeSH Endo-1,3(4)-beta-glucanase

[1] Barras, D.R. and Stone, B.A. (1969). „β-1,3-Glucan hydrolases from Euglena gracilis. I. The nature of the hydrolases”. Biochim. Biophys. Acta 191: 329-341. PMID 5354264.

[2] Barras, D.R. and Stone, B.A. (1969). „β-1,3-Glucan hydrolases from Euglena gracilis. II. Purification and properties of the β-1,3-glucan exo-hydrolase”. Biochim. Biophys. Acta 191: 342-353. PMID 5354265.

[3] Cunningham, L.W. and Manners, D.J. (1961). „Enzymic degradation of lichenin”. Biochem. J. 80: 42-42.

[4] Reese, E.T. and Mandels, M. (1959). „β-D-1,3-Glucanases in fungi”. Can. J. Microbiol. 5: 173-185. PMID 13638895.

[5] Sova, V.V., Elyakova, L.A. and Vaskovsky, V.E. (1970). „Purification and some properties of β-1,3-glucan glucanohydrolase from the crystalline style of bivalvia, Spisula sachalinensis”. Biochim. Biophys. Acta 212: 111-115. PMID 5500926.

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