Home > Publications database > Kinetic and structural details of urease inactivation by thiuram disulphides > print

001     1018321
005     20250204113738.0
024 7 _ |a 10.1016/j.jinorgbio.2023.112398
|2 doi
024 7 _ |a 0162-0134
|2 ISSN
024 7 _ |a 1873-3344
|2 ISSN
024 7 _ |a 37879152
|2 pmid
024 7 _ |a WOS:001104731700001
|2 WOS
037 _ _ |a FZJ-2023-04706
082 _ _ |a 540
100 1 _ |a Mazzei, Luca
|0 P:(DE-HGF)0
|b 0
|e Corresponding author
245 _ _ |a Kinetic and structural details of urease inactivation by thiuram disulphides
260 _ _ |a New York, NY [u.a.]
|c 2024
|b Elsevier
336 7 _ |a article
|2 DRIVER
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|b journal
|m journal
|0 PUB:(DE-HGF)16
|s 1701770054_31575
|2 PUB:(DE-HGF)
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a Journal Article
|0 0
|2 EndNote
520 _ _ |a This paper reports on the molecular details of the reactivity of urease, a nickel-dependent enzyme that catalyses the last step of organic nitrogen mineralization, with thiuram disulphides, a class of molecules known to inac- tivate the enzyme with high efficacy but for which the mechanism of action had not been yet established. IC50 values of tetramethylthiuram disulphide (TMTD or Thiram) and tetraethylthiuram disulphide (TETD or Disul- firam) in the low micromolar range were determined for plant and bacterial ureases. The X-ray crystal structure of Sporosarcina pasteurii urease inactivated by Thiram, determined at 1.68 Å resolution, revealed the presence of a covalent modification of the catalytically essential cysteine residue. This is located on the flexible flap that modulates the size of the active site channel and cavity. Formation of a Cys-S-S-C(S)-N(CH3)2 functionality responsible for enzyme inactivation was observed. Quantum-mechanical calculations carried out to rationalise the large reactivity of the active site cysteine support the view that a conserved histidine residue, adjacent to the cysteine in the active site flap, modulates the charge and electron density along the thiol S–H bond by shifting electrons towards the sulphur atom and rendering the thiol proton more reactive. We speculate that this proton could be transferred to the nickel-coordinated urea amide group to yield a molecule of ammonia from the generated Curea-NH3+ functionality during catalysis.
536 _ _ |a 5241 - Molecular Information Processing in Cellular Systems (POF4-524)
|0 G:(DE-HGF)POF4-5241
|c POF4-524
|f POF IV
|x 0
588 _ _ |a Dataset connected to CrossRef, Journals: juser.fz-juelich.de
700 1 _ |a Paul, Arundhati
|0 P:(DE-HGF)0
|b 1
700 1 _ |a Cianci, Michele
|0 P:(DE-HGF)0
|b 2
700 1 _ |a Devodier, Marta
|0 P:(DE-Juel1)198662
|b 3
|u fzj
700 1 _ |a Mandelli, Davide
|0 P:(DE-Juel1)190906
|b 4
|u fzj
700 1 _ |a Carloni, Paolo
|0 P:(DE-Juel1)145614
|b 5
|u fzj
700 1 _ |a Ciurli, Stefano
|0 P:(DE-HGF)0
|b 6
773 _ _ |a 10.1016/j.jinorgbio.2023.112398
|g Vol. 250, p. 112398 -
|0 PERI:(DE-600)1491314-8
|p 112398 -
|t Journal of inorganic biochemistry
|v 250
|y 2024
|x 0162-0134
856 4 _ |u https://juser.fz-juelich.de/record/1018321/files/Urease_Mazzei-1.pdf
|y Restricted
856 4 _ |u https://juser.fz-juelich.de/record/1018321/files/Urease_Mazzei-1.gif?subformat=icon
|x icon
|y Restricted
856 4 _ |u https://juser.fz-juelich.de/record/1018321/files/Urease_Mazzei-1.jpg?subformat=icon-1440
|x icon-1440
|y Restricted
856 4 _ |u https://juser.fz-juelich.de/record/1018321/files/Urease_Mazzei-1.jpg?subformat=icon-180
|x icon-180
|y Restricted
856 4 _ |u https://juser.fz-juelich.de/record/1018321/files/Urease_Mazzei-1.jpg?subformat=icon-640
|x icon-640
|y Restricted
909 C O |o oai:juser.fz-juelich.de:1018321
|p VDB
910 1 _ |a Forschungszentrum Jülich
|0 I:(DE-588b)5008462-8
|k FZJ
|b 3
|6 P:(DE-Juel1)198662
910 1 _ |a Forschungszentrum Jülich
|0 I:(DE-588b)5008462-8
|k FZJ
|b 4
|6 P:(DE-Juel1)190906
910 1 _ |a Forschungszentrum Jülich
|0 I:(DE-588b)5008462-8
|k FZJ
|b 5
|6 P:(DE-Juel1)145614
913 1 _ |a DE-HGF
|b Key Technologies
|l Natural, Artificial and Cognitive Information Processing
|1 G:(DE-HGF)POF4-520
|0 G:(DE-HGF)POF4-524
|3 G:(DE-HGF)POF4
|2 G:(DE-HGF)POF4-500
|4 G:(DE-HGF)POF
|v Molecular and Cellular Information Processing
|9 G:(DE-HGF)POF4-5241
|x 0
914 1 _ |y 2024
915 _ _ |a WoS
|0 StatID:(DE-HGF)0113
|2 StatID
|b Science Citation Index Expanded
|d 2023-10-21
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)1190
|2 StatID
|b Biological Abstracts
|d 2023-10-21
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0160
|2 StatID
|b Essential Science Indicators
|d 2023-10-21
915 _ _ |a Nationallizenz
|0 StatID:(DE-HGF)0420
|2 StatID
|d 2025-01-02
|w ger
915 _ _ |a JCR
|0 StatID:(DE-HGF)0100
|2 StatID
|b J INORG BIOCHEM : 2022
|d 2025-01-02
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0200
|2 StatID
|b SCOPUS
|d 2025-01-02
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0300
|2 StatID
|b Medline
|d 2025-01-02
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0600
|2 StatID
|b Ebsco Academic Search
|d 2025-01-02
915 _ _ |a Peer Review
|0 StatID:(DE-HGF)0030
|2 StatID
|b ASC
|d 2025-01-02
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0199
|2 StatID
|b Clarivate Analytics Master Journal List
|d 2025-01-02
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)1150
|2 StatID
|b Current Contents - Physical, Chemical and Earth Sciences
|d 2025-01-02
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)1050
|2 StatID
|b BIOSIS Previews
|d 2025-01-02
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)1030
|2 StatID
|b Current Contents - Life Sciences
|d 2025-01-02
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0150
|2 StatID
|b Web of Science Core Collection
|d 2025-01-02
915 _ _ |a IF < 5
|0 StatID:(DE-HGF)9900
|2 StatID
|d 2025-01-02
920 _ _ |l yes
920 1 _ |0 I:(DE-Juel1)IAS-5-20120330
|k IAS-5
|l Computational Biomedicine
|x 0
920 1 _ |0 I:(DE-Juel1)INM-9-20140121
|k INM-9
|l Computational Biomedicine
|x 1
980 _ _ |a journal
980 _ _ |a VDB
980 _ _ |a I:(DE-Juel1)IAS-5-20120330
980 _ _ |a I:(DE-Juel1)INM-9-20140121
980 _ _ |a UNRESTRICTED

LibraryCollectionCLSMajorCLSMinorLanguageAuthor
Marc 21