Substrate Specificity

"Substrate Specificity" 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

A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.

Descriptor ID	D013379
MeSH Number(s)	G02.111.835
Concept/Terms	Substrate Specificity Substrate Specificity Specificities, Substrate Specificity, Substrate Substrate Specificities

Below are MeSH descriptors whose meaning is more general than "Substrate Specificity".

Biological Sciences [G]
Chemical Phenomena [G02]
Biochemical Phenomena [G02.111]
Substrate Specificity [G02.111.835]

Below are MeSH descriptors whose meaning is related to "Substrate Specificity".

Below are MeSH descriptors whose meaning is more specific than "Substrate Specificity".

publications

Timeline | Most Recent

This graph shows the total number of publications written about "Substrate Specificity" by people in this website by year, and whether "Substrate Specificity" was a major or minor topic of these publications.

Bar chart showing 179 publications over 29 distinct years, with a maximum of 18 publications in 2006

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

Year	Minor Topic	Total
1996	6	6
1997	3	3
1998	4	4
2000	2	2
2001	3	3
2002	5	5
2003	9	9
2004	9	9
2005	14	14
2006	18	18
2007	5	5
2008	12	12
2009	10	10
2010	10	10
2011	8	8
2012	7	7
2013	6	6
2014	6	6
2015	1	1
2016	6	6
2017	9	9
2018	4	4
2019	5	5
2020	3	3
2021	6	6
2023	4	4
2024	2	2
2025	1	1
2026	1	1

Below are the most recent publications written about "Substrate Specificity" by people in Profiles.

Shirakawa KT, Parikh T, Machado LESF, Poimenidou G, Nguyen HT, Dell'Acqua ML, Kettenbach AN, Page R, Peti W. The clinical missense variant E282K in PPP3CA/calcineurin shifts substrate dephosphorylation by altering active site recruitment. Nat Commun. 2026 Feb 16; 17(1).

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Borar P, Biswas T, Chaudhuri A, Rao PT, Raychaudhuri S, Huxford T, Chakrabarti S, Ghosh G, Polley S. Dual-specific autophosphorylation of kinase IKK2 enables phosphorylation of substrate I?Ba through a phosphoenzyme intermediate. Elife. 2025 Jun 30; 13.

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Choy MS, Nguyen HT, Kumar GS, Peti W, Kettenbach AN, Page R. A protein phosphatase 1 specific phosphatase targeting peptide (PhosTAP) to identify the PP1 phosphatome. Proc Natl Acad Sci U S A. 2024 Oct 29; 121(44):e2415383121.

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Chen X, Raiff A, Li S, Guo Q, Zhang J, Zhou H, Timms RT, Yao X, Elledge SJ, Koren I, Zhang K, Xu C. Mechanism of ?-Pro/C-degron recognition by the CRL2FEM1B ubiquitin ligase. Nat Commun. 2024 Apr 26; 15(1):3558.

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Hein JB, Nguyen HT, Garvanska DH, Nasa I, Kruse T, Feng Y, Lopez Mendez B, Davey N, Kettenbach AN, Fordyce PM, Nilsson J. Phosphatase specificity principles uncovered by MRBLE:Dephos and global substrate identification. Mol Syst Biol. 2023 12 06; 19(12):e11782.

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Calhoun JC, Damania B, Griffith JD, Costantini LM. Electron microscopy mapping of the DNA-binding sites of monomeric, dimeric, and multimeric KSHV RTA protein. J Virol. 2023 10 31; 97(10):e0063723.

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Nguyen H, Kettenbach AN. Substrate and phosphorylation site selection by phosphoprotein phosphatases. Trends Biochem Sci. 2023 08; 48(8):713-725.

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Toro TB, Bornes KE, Watt TJ. Lysine Deacetylase Substrate Selectivity: Distinct Interaction Surfaces Drive Positive and Negative Selection for Residues Following Acetyllysine. Biochemistry. 2023 05 02; 62(9):1464-1483.

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Hargrove TY, Wawrzak Z, Rachakonda G, Nes WD, Villalta F, Guengerich FP, Lepesheva GI. Relaxed Substrate Requirements of Sterol 14a-Demethylase from Naegleria fowleri Are Accompanied by Resistance to Inhibition. J Med Chem. 2021 12 09; 64(23):17511-17522.

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Toro TB, Swanier JS, Bezue JA, Broussard CG, Watt TJ. Lysine Deacetylase Substrate Selectivity: A Dynamic Ionic Interaction Specific to KDAC8. Biochemistry. 2021 08 24; 60(33):2524-2536.

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