Cellobiohydrolase
From Proteopedia
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== Function == | == Function == | ||
| - | '''Cellobiohydrolase''' (CBH) is a cellulase which degrades cellulose by hydrolysing the 1,4-β-D-glycosidic bonds. CBH is an exocellulase which cleaves two to four units from the ends of cellulose. There are two types of CBH. '''CBHI''' cleaves progressively from the reducing end while '''CBHII''' cleaves progressively from the nonreducing end of cellulose.<ref>PMID:9466911</ref>. The exo-acting CBH I is called '''Cel7A'''. The endo-acting CBH I is called '''Cel7B'''. '''Cellobiohydrolase Cel6A''' contains an active site within a tunnel which opens and closes in response to ligand binding | + | '''Cellobiohydrolase''' (CBH) is a cellulase which degrades cellulose by hydrolysing the 1,4-β-D-glycosidic bonds. CBH is an exocellulase which cleaves two to four units from the ends of cellulose. There are two types of CBH. '''CBHI''' cleaves progressively from the reducing end while '''CBHII''' cleaves progressively from the nonreducing end of cellulose.<ref>PMID:9466911</ref>. The exo-acting CBH I is called '''Cel7A'''. The endo-acting CBH I is called '''Cel7B'''. '''Cellobiohydrolase Cel6A''' contains an active site within a tunnel which opens and closes in response to ligand binding<ref>PMID:12842048</ref>. |
==Structural highlights == | ==Structural highlights == | ||
Revision as of 09:57, 5 May 2019
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References
- ↑ Divne C, Stahlberg J, Teeri TT, Jones TA. High-resolution crystal structures reveal how a cellulose chain is bound in the 50 A long tunnel of cellobiohydrolase I from Trichoderma reesei. J Mol Biol. 1998 Jan 16;275(2):309-25. PMID:9466911 doi:http://dx.doi.org/10.1006/jmbi.1997.1437
- ↑ Varrot A, Frandsen TP, von Ossowski I, Boyer V, Cottaz S, Driguez H, Schulein M, Davies GJ. Structural basis for ligand binding and processivity in cellobiohydrolase Cel6A from Humicola insolens. Structure. 2003 Jul;11(7):855-64. PMID:12842048
- ↑ Stahlberg J, Divne C, Koivula A, Piens K, Claeyssens M, Teeri TT, Jones TA. Activity studies and crystal structures of catalytically deficient mutants of cellobiohydrolase I from Trichoderma reesei. J Mol Biol. 1996 Nov 29;264(2):337-49. PMID:8951380 doi:http://dx.doi.org/10.1006/jmbi.1996.0644
