The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Roles of the Catalytic Domain and Two Cellulose Binding Domains of Thermomonospora fusca E4 in Cellulose Hydrolysis
Open accessAbstract
Thermomonospora fusca E4 is an unusual 90.4-kDa endocellulase comprised of a catalytic domain (CD), an internal family IIIc cellulose binding domain (CBD), a fibronectinlike domain, and a family II CBD. Constructs containing the CD alone (E4-51), the CD plus the family IIIc CBD (E4-68), and the CD plus the fibronectinlike domain plus the family II CBD (E4-74) were made by using recombinant DNA techniques. The activities of each purified protein on bacterial microcrystalline cellulose (BMCC), filter paper, swollen cellulose, and carboxymethyl cellulose were measured. Only the whole enzyme, E4-90, could reach the target digestion of 4.5% on filter paper. Removal of the internal family IIIc CBD (E4-51 and E4-74) decreased activity markedly on every substrate. E4-74 did bind to BMCC but had almost no hydrolytic activity, while E4-68 retained 32% of the activity on BMCC even though it did not bind. A low-activity mutant of one of the catalytic bases, E4-68 (Asp55Cys), did bind to BMCC, although E4-51 (Asp55Cys) did not. The ratios of soluble to insoluble reducing sugar produced after filter paper hydrolysis by E4-90, E4-68, E4-74, and E4-51 were 6.9, 3.5, 1.3, and 0.6, respectively, indicating that the family IIIc CBD is important for E4 processivity.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
The relation between the divergence of sequence and structure in proteins.
Chothia, C., & Lesk, A. M. (1986) · The EMBO Journal · doi:10.1002/j.1460-2075.1986.tb04288.x · Cited by 2,458
Cited by
Microbial Cellulose Utilization: Fundamentals and Biotechnology
Lynd, L. R., Weimer, P. J., van Zyl, W. H., & Pretorius, I. S. (2002) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.66.3.506-577.2002 · Cited by 4,726
Payne, C. M., Knott, B. C., Mayes, H. B., Hansson, H., Himmel, M. E., Sandgren, M., Ståhlberg, J., & Beckham, G. T. (2015) · Chemical Reviews · doi:10.1021/cr500351c · Cited by 855
The prospects of cellulase-producing bacteria for the bioconversion of lignocellulosic biomass
Maki, M., Leung, K. T., & Qin, W. (2009) · International Journal of Biological Sciences · doi:10.7150/ijbs.5.500 · Cited by 559
Costs and benefits of processivity in enzymatic degradation of recalcitrant polysaccharides
Horn, S. J., Sikorski, P., Cederkvist, J. B., Vaaje-Kolstad, G., Sørlie, M., Synstad, B., Vriend, G., Vårum, K. M., & Eijsink, V. G. H. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608909103 · Cited by 277
Metadata
- Authors
- Irwin, D., Shin, D.-H., Zhang, S., Barr, B. K., Sakon, J., Karplus, P. A., & Wilson, D. B.
- Venue
- Journal of Bacteriology
- Publisher
- American Society for Microbiology
- Published
- 1998-04
- Volume
- 180
- Issue
- 7
- Pages
- 1709-1714
- ISSN
- 0021-9193 (ISSN-L)
- 1098-5530
- OpenAlex
- W2170765652
- Cited by
- 200
- References
- 1
- FWCI
- 9.41
- Type
- journal article
- Language
- en
- Open access
- bronze
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Roles of the Catalytic Domain and Two Cellulose Binding Domains of Thermomonospora fusca E4 in Cellulose Hydrolysis. https://app.cochat.ai/papers/10.1128/jb.180.7.1709-1714.1998
- The paper
- Irwin, D., Shin, D.-H., Zhang, S., Barr, B. K., Sakon, J., Karplus, P. A., & Wilson, D. B. (1998). Roles of the Catalytic Domain and Two Cellulose Binding Domains of Thermomonospora fusca E4 in Cellulose Hydrolysis. Journal of Bacteriology. https://doi.org/10.1128/jb.180.7.1709-1714.1998
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
