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.

MeSH information

Definition | Details | More General Concepts | Related Concepts | More Specific Concepts

The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.

Descriptor ID	D020134
MeSH Number(s)	G02.111.570.120.704 G02.111.570.820.709.275.750.188
Concept/Terms	Catalytic Domain Catalytic Domain Catalytic Domains Domain, Catalytic Domains, Catalytic Catalytic Subunit Catalytic Subunits Subunit, Catalytic Subunits, Catalytic Catalytic Region Catalytic Regions Region, Catalytic Regions, Catalytic Catalytic Core Catalytic Cores Core, Catalytic Cores, Catalytic Active Site Active Site Active Sites Site, Active Sites, Active Catalytic Site Catalytic Sites Site, Catalytic Sites, Catalytic Reactive Site Reactive Sites Site, Reactive Sites, Reactive

Below are MeSH descriptors whose meaning is more general than "Catalytic Domain".

Biological Sciences [G]
Chemical Phenomena [G02]
Biochemical Phenomena [G02.111]
Molecular Structure [G02.111.570]
Binding Sites [G02.111.570.120]
Catalytic Domain [G02.111.570.120.704]
Molecular Conformation [G02.111.570.820]
Protein Conformation [G02.111.570.820.709]
Protein Structural Elements [G02.111.570.820.709.275]
Protein Domains [G02.111.570.820.709.275.750]
Catalytic Domain [G02.111.570.820.709.275.750.188]

Below are MeSH descriptors whose meaning is related to "Catalytic Domain".

Below are MeSH descriptors whose meaning is more specific than "Catalytic Domain".

publications

Timeline | Most Recent

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.

Bar chart showing 57 publications over 24 distinct years, with a maximum of 7 publications in 2015

To see the data from this visualization as text, click here.

Year	Major Topic	Minor Topic	Total
1998	0	1	1
1999	0	1	1
2000	0	1	1
2002	0	1	1
2003	1	2	3
2004	0	3	3
2005	0	3	3
2006	0	3	3
2007	1	1	2
2008	0	1	1
2009	0	4	4
2010	0	3	3
2011	0	2	2
2012	1	2	3
2013	0	5	5
2014	0	1	1
2015	2	5	7
2016	0	1	1
2017	0	1	1
2019	0	3	3
2020	0	2	2
2021	1	2	3
2022	0	1	1
2025	0	2	2

Below are the most recent publications written about "Catalytic Domain" by people in Profiles.

Lancaster EB, Hardtke HA, Melkonian TR, Venkat Ramani M, Johnson WH, Baas BJ, Zhang YJ, Whitman CP. Conversion of Inactive Non-Pro1 Tautomerase Superfamily Members into Active Tautomerases: Analysis of the Pro1 Mutants. Biochemistry. 2025 02 18; 64(4):812-822.

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Smith-Pillet ES, Billur R, Langelier MF, Talele TT, Pascal JM, Black BE. A PARP2 active site helix melts to permit DNA damage-induced enzymatic activation. Mol Cell. 2025 Mar 06; 85(5):865-876.e4.

View in: PubMed
Rouleau-Turcotte ?, Krastev DB, Pettitt SJ, Lord CJ, Pascal JM. Captured snapshots of PARP1 in the active state reveal the mechanics of PARP1 allostery. Mol Cell. 2022 08 18; 82(16):2939-2951.e5.

View in: PubMed
Rashid I, Hammel M, Sverzhinsky A, Tsai MS, Pascal JM, Tainer JA, Tomkinson AE. Direct interaction of DNA repair protein tyrosyl DNA phosphodiesterase 1 and the DNA ligase III catalytic domain is regulated by phosphorylation of its flexible N-terminus. J Biol Chem. 2021 Aug; 297(2):100921.

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Baas BJ, Medellin BP, LeVieux JA, Erwin K, Lancaster EB, Johnson WH, Kaoud TS, Moreno RY, de Ruijter M, Babbitt PC, Zhang YJ, Whitman CP. Kinetic and Structural Analysis of Two Linkers in the Tautomerase Superfamily: Analysis and Implications. Biochemistry. 2021 06 08; 60(22):1776-1786.

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Ogden TEH, Yang JC, Schimpl M, Easton LE, Underwood E, Rawlins PB, McCauley MM, Langelier MF, Pascal JM, Embrey KJ, Neuhaus D. Dynamics of the HD regulatory subdomain of PARP-1; substrate access and allostery in PARP activation and inhibition. Nucleic Acids Res. 2021 02 26; 49(4):2266-2288.

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Shao Z, Lee BJ, Rouleau-Turcotte ?, Langelier MF, Lin X, Estes VM, Pascal JM, Zha S. Clinical PARP inhibitors do not abrogate PARP1 exchange at DNA damage sites in vivo. Nucleic Acids Res. 2020 09 25; 48(17):9694-9709.

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Chan TO, Armen RS, Yadav S, Shah S, Zhang J, Tiegs BC, Keny N, Blumhof B, Deshpande DA, Rodeck U, Penn RB. A tripartite cooperative mechanism confers resistance of the protein kinase A catalytic subunit to dephosphorylation. J Biol Chem. 2020 03 06; 295(10):3316-3329.

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Black SJ, Ozdemir AY, Kashkina E, Kent T, Rusanov T, Ristic D, Shin Y, Suma A, Hoang T, Chandramouly G, Siddique LA, Borisonnik N, Sullivan-Reed K, Mallon JS, Skorski T, Carnevale V, Murakami KS, Wyman C, Pomerantz RT. Molecular basis of microhomology-mediated end-joining by purified full-length Pol?. Nat Commun. 2019 09 27; 10(1):4423.

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Supsrisunjai C, Hsu CK, Michael M, Duval C, Lee JYW, Yang HS, Huang HY, Chaikul T, Onoufriadis A, Steiner RA, Ari?ns RAS, Sarig O, Sprecher E, Eskin-Schwartz M, Samlaska C, Simpson MA, Calonje E, Parsons M, McGrath JA. Coagulation Factor XIII-A Subunit Missense Mutation in the Pathobiology of Autosomal Dominant Multiple Dermatofibromas. J Invest Dermatol. 2020 03; 140(3):624-635.e7.

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