Homologues of catalytic domains of Cellulomonas glucanases found in fungal and Bacillus glycosidases
- PMID: 2500377
- DOI: 10.1016/0378-1097(89)90479-5
Homologues of catalytic domains of Cellulomonas glucanases found in fungal and Bacillus glycosidases
Abstract
We demonstrate homology between the catalytic domains of exoglucanase (1,4-beta-D-glucan cellobiohydrolase, EC 3.2.1.91) from Cellulomonas fimi and those of endoxylanases (1,4-beta-D-xylan xylanohydrolases, EC 3.2.1.8) from Bacillus sp. strain C-125 and the fungus Cryptococcus albidus; and between the catalytic domains of endoglucanase (1,4-(1,3:1,4)-beta-D-glucan 4-glucanohydrolase, EC 3.2.1.4) from Cellulomonas fimi and exoglucanase II from Trichoderma reesei. These five enzymes apparently evolved by reshuffling of two catalytic domains and several substrate-binding domains.
Similar articles
-
Cellobiohydrolase B, a second exo-cellobiohydrolase from the cellulolytic bacterium Cellulomonas fimi.Biochem J. 1995 Oct 1;311 ( Pt 1)(Pt 1):67-74. doi: 10.1042/bj3110067. Biochem J. 1995. PMID: 7575482 Free PMC article.
-
Structural and functional relationships in two families of beta-1,4-glycanases.Eur J Biochem. 1991 Dec 5;202(2):367-77. doi: 10.1111/j.1432-1033.1991.tb16384.x. Eur J Biochem. 1991. PMID: 1761039
-
Glutamic acid 274 is the nucleophile in the active site of a "retaining" exoglucanase from Cellulomonas fimi.J Biol Chem. 1991 Aug 25;266(24):15621-5. J Biol Chem. 1991. PMID: 1678739
-
Mechanisms of cellulases and xylanases.Biochem Soc Trans. 1998 May;26(2):156-60. doi: 10.1042/bst0260156. Biochem Soc Trans. 1998. PMID: 9649739 Review. No abstract available.
-
Structural and functional properties of low molecular weight endo-1,4-beta-xylanases.J Biotechnol. 1997 Sep 16;57(1-3):137-49. doi: 10.1016/s0168-1656(97)00095-3. J Biotechnol. 1997. PMID: 9335170 Review.
Cited by
-
Cloning, sequence analysis, and expression of genes encoding xylan-degrading enzymes from the thermophile "Caldocellum saccharolyticum".Appl Environ Microbiol. 1990 Apr;56(4):1017-24. doi: 10.1128/aem.56.4.1017-1024.1990. Appl Environ Microbiol. 1990. PMID: 2111111 Free PMC article.
-
Spatial separation of protein domains is not necessary for catalytic activity or substrate binding in a xylanase.Biochem J. 1990 Jul 1;269(1):261-4. doi: 10.1042/bj2690261. Biochem J. 1990. PMID: 2115772 Free PMC article.
-
Characterization and sequencing of an active-site cysteine-containing peptide from the xylanase of a thermotolerant Streptomyces.Biochem J. 1992 Feb 1;281 ( Pt 3)(Pt 3):601-5. doi: 10.1042/bj2810601. Biochem J. 1992. PMID: 1536641 Free PMC article.
-
Characterization of hybrid proteins consisting of the catalytic domains of Clostridium and Ruminococcus endoglucanases, fused to Pseudomonas non-catalytic cellulose-binding domains.Biochem J. 1991 Nov 1;279 ( Pt 3)(Pt 3):787-92. doi: 10.1042/bj2790787. Biochem J. 1991. PMID: 1953672 Free PMC article.
-
Structural environment of an essential cysteine residue of xylanase from Chainia sp. (NCL 82.5.1).Biochem J. 1996 Jun 15;316 ( Pt 3)(Pt 3):771-5. doi: 10.1042/bj3160771. Biochem J. 1996. PMID: 8670151 Free PMC article.
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources