User talk:Rohet31/sandbox
Cellulase
The article describes the category of enzymes called Cellulase, consisting information related to the structure, classification, reaction mechanisms and uses. Notability of the article is reflected on the details which were sourced mainly from journal articles. Reference 6, an article, discusses about enzymatic components and corresponding functions of a bacterial species. This supports information in the ‘Types and Action’ section of the article. Evidence about the structure and classification into families and clans can be extracted from reference 8. The article, although published in 1998, contains information about Cellulosomes, a complex structure of multiple cellulases. The general details are coherent with the specific structural information in reference 6. References 9 and 10 are both journal articles detailing the medical use of cellulase in degrading bacterial growths called biofilms. The information sources mentioned are scholarly articles and can be found in the University of British Columbia Library.
The section titled ‘Structure’ consists of information about fungal and bacterial cellulases with a single structural example for each type. The 3-dimensional structure of the enzyme depends on different levels of protein structures. The number of protein structures interacting with each other is not limited to a 2-domain structure for fungal and a 5 sub-unit structure for bacterial cellulases. The Thermotoga maritima species consists of 2 beta-sheets (protein structures) surrounding a central catalytic region called the active-site.[1] Different species in the same family as T. Maritima adopts different structures. Cellulases produced by the species Coprinopsis Cinerea consists of seven protein strands in the shape of an enclosed tunnel called a beta/alpha barrel.[2] Furthermore, information regarding the effect of protein structure on the interaction between enzyme active site and the substrate (cellulose) is missing.
Additional factors like temperature, pH and metal ions influence the non-covalent interactions between enzyme structure.[3] Consequently, the enzyme-substrate reactions are affected. The number of sub-units making up cellulosomes can also determine the rate of enzyme activity.[4] These structural details were not found in the reference sources. Inclusion of this information will provide readers more detail on cellulase structures and their roles in enzyme function.
--Rohet31 (talk) 06:58, 28 September 2017 (UTC)
Henry's Peer Review
[edit]Structurally, these edits are rationally placed inside its own heading, going from simple explanations to more complex examples, and the branch-off topic having its own subheading. The placement within the article is also logical, coming after a general overview of these enzymes and their types, but before more specific information.
The main point this section seems to be trying to make is that protein structure affects the function of the cellulase, but that there is still structural variation in bacterial and fungal cellulases. The content in this edit is mainly relevant and supports this point, but there are a few places where a little bit more detail could be appreciated by readers. The line mentioning the variation in cellulase structure within the Thermotoga genus is relevant in the context presented, but there are no examples given nor references cited. Furthermore, some detail regarding how the cellulase structures (of the diverse examples given) affect their activity, or perhaps the conditions that caused their evolution to that form, could drive home the main point of this section. Related to the content, there are no issues with the sources made reference to, aside from the one unsubstantiated statement about the Thermagota genus's cellulases. The sources are diverse, and this writeup does not appear to be pushing a particular viewpoint.
The writing in this article is easily understood, but there are a few places where the flow could be improved. Keeping the more general information together by moving the portion of the second article mentioning changes in the amino-acid sequence relating to enzymatic changes above the examples of different species cellulase structure. This way the examples will not interrupt the flow of the general information. Adjusting the names of the species mentioned into the standard ‘’Genus species’’ and ‘’G. species’’ could help someone not familiar with bacterial naming to understand what those are.
Stbox4 (talk) 02:14, 8 November 2017 (UTC)
- ^ http://onlinelibrary.wiley.com/doi/10.1002/prot.22953/full.
{{cite journal}}: Cite journal requires|journal=(help); Missing or empty|title=(help) - ^ Liu, Yuan; Yoshida, Makoto; Kurakata, Yuma; Miyazaki, Takatsugu; Igarashi, Kiyohiko; Samejima, Masahiro; Fukuda, Kiyoharu; Nishikawa, Atsushi; Tonozuka, Takashi (1 March 2010). "Crystal structure of a glycoside hydrolase family 6 enzyme, CcCel6C, a cellulase constitutively produced by Coprinopsis cinerea". FEBS Journal. 277 (6): 1532–1542. doi:10.1111/j.1742-4658.2010.07582.x. ISSN 1742-4658.
{{cite journal}}: no-break space character in|title=at position 120 (help) - ^ Lee, You-Jung; Kim, Bo-Kyung; Lee, Bo-Hwa; Jo, Kang-Ik; Lee, Nam-Kyu; Chung, Chung-Han; Lee, Young-Choon; Lee, Jin-Woo (1 January 2008). "Purification and characterization of cellulase produced by Bacillus amyoliquefaciens DL-3 utilizing rice hull". Bioresource Technology. 99 (2): 378–386. doi:10.1016/j.biortech.2006.12.013.
- ^ Tsai, Shen-Long; DaSilva, Nancy A.; Chen, Wilfred (18 January 2013). "Functional Display of Complex Cellulosomes on the Yeast Surface via Adaptive Assembly". ACS Synthetic Biology. 2 (1): 14–21. doi:10.1021/sb300047u.