Identification of the Catalytic Residues in the Cyclase Domain of the Class IV Lanthipeptide Synthetase SgbL
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Bibliographic citation
-
In: ChemBioChem (22:22) - Weinheim : Wiley-VCH - S. 3169-3172
- Event
-
Veröffentlichung
- (where)
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Berlin
- (who)
-
Technische Universität Berlin
- (when)
-
2023
- Creator
-
Hegemann, Julian D.
Süssmuth, Roderich D.
- DOI
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10.14279/depositonce-18793
- Handle
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11303/19995
- URN
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urn:nbn:de:101:1-2023091301593908816696
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
25.03.2025, 1:56 PM CET
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Hegemann, Julian D.
- Süssmuth, Roderich D.
- Technische Universität Berlin
Time of origin
- 2023
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The role of soluble guanylate cyclase in metabolism
Some properties of the quadratic residues of primes.
On the law of reciprocity of quadratic residues.
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Crystal structure of the catalytic domains of membranous adenylyl cyclase with MANT-ITP and electrophysiological analysis of MANT nucleotides in cardiomyocytes
Processing strategy for catalytic residues containing vanadium
Structural characterisation of the catalytic core of the class III adenylyl cyclase Rv0386 from mycobacterium tuberculosis
Deciphering the Catalytic Mechanism of the Zn Enzyme Glutaminyl Cyclase and the Deduction of Transition-State Analog Inhibitors
Identification of amino acid residues essential for the catalytic activity of Drosophila P. element transposase
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The role of soluble guanylate cyclase in metabolism
Some properties of the quadratic residues of primes.
On the law of reciprocity of quadratic residues.
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