 Catalytic Domain
"Catalytic Domain" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.
| Descriptor ID |
D020134
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| MeSH Number(s) |
G02.111.570.120.704 G02.111.570.790.709.610.189
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| Concept/Terms |
Catalytic Domain- Catalytic Domain
- Catalytic Domains
- Domain, Catalytic
- Domains, Catalytic
- Catalytic Region
- Catalytic Regions
- Region, Catalytic
- Regions, Catalytic
- Catalytic Subunit
- Catalytic Subunits
- Subunit, Catalytic
- Subunits, Catalytic
- Catalytic Core
- Catalytic Cores
- Core, Catalytic
- Cores, Catalytic
Active Site- Active Site
- Active Sites
- Site, Active
- Sites, Active
- Reactive Site
- Reactive Sites
- Site, Reactive
- Sites, Reactive
- Catalytic Site
- Catalytic Sites
- Site, Catalytic
- Sites, Catalytic
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Below are MeSH descriptors whose meaning is more general than "Catalytic Domain".
Below are MeSH descriptors whose meaning is more specific than "Catalytic Domain".
This graph shows the total number of publications written about "Catalytic Domain" by people in this website by year, and whether "Catalytic Domain" was a major or minor topic of these publications.
To see the data from this visualization as text, click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 1998 | 0 | 1 | 1 | | 1999 | 0 | 2 | 2 | | 2000 | 1 | 2 | 3 | | 2001 | 1 | 3 | 4 | | 2002 | 0 | 2 | 2 | | 2003 | 0 | 5 | 5 | | 2004 | 0 | 1 | 1 | | 2005 | 0 | 5 | 5 | | 2006 | 0 | 6 | 6 | | 2007 | 0 | 3 | 3 | | 2008 | 0 | 5 | 5 | | 2009 | 0 | 8 | 8 | | 2010 | 0 | 7 | 7 | | 2011 | 2 | 10 | 12 | | 2012 | 1 | 6 | 7 | | 2013 | 0 | 4 | 4 | | 2014 | 0 | 10 | 10 | | 2015 | 3 | 10 | 13 | | 2016 | 0 | 6 | 6 | | 2017 | 0 | 7 | 7 | | 2018 | 1 | 4 | 5 | | 2019 | 0 | 7 | 7 | | 2020 | 1 | 3 | 4 |
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Below are the most recent publications written about "Catalytic Domain" by people in Profiles.
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Kim Y, Jedrzejczak R, Maltseva NI, Wilamowski M, Endres M, Godzik A, Michalska K, Joachimiak A. Crystal structure of Nsp15 endoribonuclease NendoU from SARS-CoV-2. Protein Sci. 2020 07; 29(7):1596-1605.
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Hiller DA, Dunican BF, Nallur S, Li NS, Piccirilli JA, Strobel SA. The Positively Charged Active Site of the Bacterial Toxin RelE Causes a Large Shift in the General Base pKa. Biochemistry. 2020 05 05; 59(17):1665-1671.
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Bloch JS, Pesciullesi G, Boilevin J, Nosol K, Irobalieva RN, Darbre T, Aebi M, Kossiakoff AA, Reymond JL, Locher KP. Structure and mechanism of the ER-based glucosyltransferase ALG6. Nature. 2020 03; 579(7799):443-447.
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Ganguly A, Weissman BP, Giese TJ, Li NS, Hoshika S, Rao S, Benner SA, Piccirilli JA, York DM. Confluence of theory and experiment reveals the catalytic mechanism of the Varkud satellite ribozyme. Nat Chem. 2020 02; 12(2):193-201.
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Gaines CS, Piccirilli JA, York DM. The L-platform/L-scaffold framework: a blueprint for RNA-cleaving nucleic acid enzyme design. RNA. 2020 02; 26(2):111-125.
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Prakash P, Gorfe AA. Probing the Conformational and Energy Landscapes of KRAS Membrane Orientation. J Phys Chem B. 2019 10 17; 123(41):8644-8652.
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Wan H, Gao J, Yang H, Yang S, Harvey R, Chen YQ, Zheng NY, Chang J, Carney PJ, Li X, Plant E, Jiang L, Couzens L, Wang C, Strohmeier S, Wu WW, Shen RF, Krammer F, Cipollo JF, Wilson PC, Stevens J, Wan XF, Eichelberger MC, Ye Z. The neuraminidase of A(H3N2) influenza viruses circulating since 2016 is antigenically distinct from the A/Hong Kong/4801/2014 vaccine strain. Nat Microbiol. 2019 12; 4(12):2216-2225.
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Fang X, Osipiuk J, Chakravarthy S, Yuan M, Menzer WM, Nissen D, Liang P, Raba DA, Tuz K, Howard AJ, Joachimiak A, Minh DDL, Juarez O. Conserved residue His-257 of Vibrio cholerae flavin transferase ApbE plays a critical role in substrate binding and catalysis. J Biol Chem. 2019 09 13; 294(37):13800-13810.
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Berntsson O, Rodriguez R, Henry L, Panman MR, Hughes AJ, Einholz C, Weber S, Ihalainen JA, Henning R, Kosheleva I, Schleicher E, Westenhoff S. Photoactivation of Drosophila melanogaster cryptochrome through sequential conformational transitions. Sci Adv. 2019 07; 5(7):eaaw1531.
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Wilson TJ, Liu Y, Li NS, Dai Q, Piccirilli JA, Lilley DMJ. Comparison of the Structures and Mechanisms of the Pistol and Hammerhead Ribozymes. J Am Chem Soc. 2019 05 15; 141(19):7865-7875.
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