Cellulomonas fimi

Cellulomonas fimi Endoglucanase A (i7) Microbispora bispora Endoglucanase I (5) Streptomyces sp. Cellulase A (72) Trichoderma reesei Cellobiohydrolase II (75)... 

Langsford et al. reported that Cellulomonas fimi culture supernatants contained cellulase and proteinase activities, for which there appeared to be a relationship. Glucose repressed the synthesis of both activities and cellulose induced both 60), Adding cellulose to Cellulomonas sp. (NRCC 2406) cultures stimulated growth and improved production of cellulases 61). Optimum conditions for growth and cellulase production were pH 6.5 and 30 C. The addition of glucose in the presence of cellulose inhibited growth. Several species of Cellulomonas have cellobiose phosphorylase. 

Structural Functional Organization of Cellulomonas fimi P-1, 4-Glucanases... 

Cellulomonas fimi endoglucanase CenA PT2S(PT)4T(PT)7VTPQPT 7... 

Figure 1. Amino acid sequences of microbial glycohydrolases. A Aureobasid-iwn sp. endo-xylanase Sc Schizophyllwn commune endo-xylanase C Chainia sp. endo-xylanase Bp Bacillus pumilus endo-xylanase Bs Bacillus subtilis Bacillus circulans endo-xylanase Pf Pseudomonas fluorescens endo-xylanase B alkalophilic Bacillus sp. endo-xylanase Ct Clostridium thermocellum endo-xylanase Cf Cellulomonas fimi cellobiohydrolase Ca Cryptococcus albidus endo-xylanase. Residue numbers are those of the adjacent residue, counting from the N-terminus of the mature protein.

Family 10 xylanase Cex from Cellulomonas fimi and family 11 xylanase Bex from Bacillus circulans198,199 (the first being an anti-, the second a syn-protonator) were exposed to deoxynojirimycin-related (80, Scheme 22) and isofagomine analogous (81) xylosidase inhibitors, along with the anti-protonation-selective xylobiosyl... 

V. Notenboom, S. J. Williams, R. Hoos, S. G. Withers, and D. R. Rose, Detailed structural analysis of glycosidase/inhibitor interactions Complexes of Cex from Cellulomonas fimi with xylobiose-derived aza-sugars, Biochemistry, 39 (2000) 11553—11563. 

The core-enzymes, prepared in our laboratory, and containing the active centers, were successfully crystallized (Dr. Jones, Uppsala, communicated) and tertiary structures will be described in the near future. Chemical modification studies on these enzymes are currently being undertaken in our laboratory identification of important catalytic residues and location of the active centers will lead to more functional information on these enzymes. Other cellulases such as some endoglucanases from Clostridium thermocel-lum (EG A, EG B, EG D) (10) and EngA and Exg from Cellulomonas fimi (19) also contain sequences of conserved, terminally located and sometimes reiterated, amino acids. Some of these sequences are preceded by proline-serine rich domains. Thus, a bistructural-bifunctional organization seems to be a rather common feature among cellulases, at least for EngA and Exg from C. fimi and the enzymes from Trichoderma reesei. 

Creagh, A. L., Ong, E., Jervis, E., Kilbum, D. G., and Haynes, C. A. 1996. Binding of the cellulose-binding domain of exoglucanase Cex from Cellulomonas fimi to insoluble microcrystalline cellulose is entropically driven. Proc. Natl. Acad. Sci., 93, 12229-12234. 

CenA) from Cellulomonas-Fimi—Evidence for the Involvement of Tryptophan Residues in Binding. Mol. Microbio., 11,747-755. 

Recently, Hekmat et al.115 reported the synthesis of novel sugar probes that are based on a l-(2,4-dinitrophenyl)-2-fluorosugar inhibitor that traps the catalytic nucleophile of inverting /3-glycosidases (Figure 19(b)). This probe was successfully applied to profde several glycosidases in the extracellular proteome of the soil bacterium Cellulomonas fimi by MS methods. 

GH 2 P-mannosidase, acid-base mutant Cellulomonas fimi E429A 1.12, 1.17 (N3-) 211... 

The role of CBMs may not be entirely passive, although thermodynamics ensure that any interaction has to be stoichiometric rather than catalytic. An isolated CBM 2a, originally from a Cellulomonas fimi endoglucanase, formed the usual (3-sandwich, but, in solution, when unconstrained by an attached catalytic domain, dimerised." This CBM liberated small particles from cotton linters but not bacterial microcrystalline cellulose the same behaviour was shown by the holoenzyme which had been inactivated with the appropriate Withers inactivator." " However, another CBM 2a, from Cellvibrio japonicus, was rigorously shown to act only by increasing substrate proximity." ... 

SJ-l-Methyl arylalkylamines (SJ-Arylalkyl acylamidases Nocardia erythropolis, Cellulomonas fimi... 

Khanna, S., Gauri, P. (1993). Regulation, purification and properties of xylanase from Cellulomonas fimi. Enzyme and Microbial Technology, 15, 990-995. 

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