N‐terminal modifications of cellular proteins: The enzymes involved, their substrate specificities and biological effects
The vast majority of eukaryotic proteins are N‐terminally modified by one or more processing enzymes. Enzymes acting on the very first amino acid of a polypeptide include different peptidases, transferases, and ligases. Methionine aminopeptidases excise the initiator methionine leaving the nascent polypeptide with a newly exposed amino acid that may be further modified. N‐terminal acetyl‐, methyl‐, myristoyl‐, and palmitoyltransferases may attach an acetyl, methyl, myristoyl, or palmitoyl group, respectively, to the α‐amino group of the target protein N‐terminus. With the action of ubiquitin ligases, one or several ubiquitin molecules are transferred, and hence, constitute the N‐terminal modification. Modifications at protein N‐termini represent an important contribution to proteomic diversity and complexity, and are essential for protein regulation and cellular signaling. Consequently, dysregulation of the N‐terminal modifying enzymes is implicated in human diseases. We here review the different protein N‐terminal modifications occurring co‐ or post‐translationally with emphasis on the responsible enzymes and their substrate specificities.
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Bibliographic citation
-
N‐terminal modifications of cellular proteins: The enzymes involved, their substrate specificities and biological effects ; volume:15 ; number:14 ; year:2015 ; pages:2385-2401 ; extent:17
Proteomics ; 15, Heft 14 (2015), 2385-2401 (gesamt 17)
- Creator
-
Varland, Sylvia
Osberg, Camilla
Arnesen, Thomas
- DOI
-
10.1002/pmic.201400619
- URN
-
urn:nbn:de:101:1-2022112407311473434778
- Rights
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
17.04.2032, 7:33 AM CEST
Data provider
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Varland, Sylvia
- Osberg, Camilla
- Arnesen, Thomas
Other Objects (12)
Reconstructing molecular evolution by changing substrate specificities within the amidohydrolase superfamily of enzymes
Reconstructing molecular evolution by changing substrate specificities within the amidohydrolase superfamily of enzymes
Threonine aldolases: perspectives in engineering and screening the enzymes with enhanced substrate and stereo specificities
Reassessment of chitosanase substrate specificities and classification
Individual functions and substrate specificities of importin α subtypes
Bacillus subtilis 5′-nucleotidases with various functions and substrate specificities
Synthetic and biological approaches to map substrate specificities of proteases
Substrate specificities of baking lipases for use in fine bakery goods
Trigger Factor and DnaK possess overlapping substrate pools and binding specificities
The papain-like cysteine proteinases NbCysP6 and NbCysP7 are highly processive enzymes with substrate specificities complementary to Nicotiana benthamiana cathepsin B
Substrate Modifications for Stability Improvements of Flexible Perovskite Solar Cells
Modifications of diketopiperazines assembled by cyclodipeptide synthases with cytochrome P450 enzymes
Reconstructing molecular evolution by changing substrate specificities within the amidohydrolase superfamily of enzymes
Reconstructing molecular evolution by changing substrate specificities within the amidohydrolase superfamily of enzymes
Threonine aldolases: perspectives in engineering and screening the enzymes with enhanced substrate and stereo specificities
Reassessment of chitosanase substrate specificities and classification
Individual functions and substrate specificities of importin α subtypes
Bacillus subtilis 5′-nucleotidases with various functions and substrate specificities
Synthetic and biological approaches to map substrate specificities of proteases
Substrate specificities of baking lipases for use in fine bakery goods
Trigger Factor and DnaK possess overlapping substrate pools and binding specificities
The papain-like cysteine proteinases NbCysP6 and NbCysP7 are highly processive enzymes with substrate specificities complementary to Nicotiana benthamiana cathepsin B
Substrate Modifications for Stability Improvements of Flexible Perovskite Solar Cells
Modifications of diketopiperazines assembled by cyclodipeptide synthases with cytochrome P450 enzymes
Reconstructing molecular evolution by changing substrate specificities within the amidohydrolase superfamily of enzymes
Reconstructing molecular evolution by changing substrate specificities within the amidohydrolase superfamily of enzymes
Threonine aldolases: perspectives in engineering and screening the enzymes with enhanced substrate and stereo specificities
Reassessment of chitosanase substrate specificities and classification
Individual functions and substrate specificities of importin α subtypes
Bacillus subtilis 5′-nucleotidases with various functions and substrate specificities
Synthetic and biological approaches to map substrate specificities of proteases
Substrate specificities of baking lipases for use in fine bakery goods
Trigger Factor and DnaK possess overlapping substrate pools and binding specificities
The papain-like cysteine proteinases NbCysP6 and NbCysP7 are highly processive enzymes with substrate specificities complementary to Nicotiana benthamiana cathepsin B
Substrate Modifications for Stability Improvements of Flexible Perovskite Solar Cells