Journal Article

PUBDB-2024-07237

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png A closer look at molecular mechanisms underlying inhibition of S -adenosyl- l -homocysteine hydrolase by transition metal cations

Gawel, M. ; Malecki, P. H. ; Sliwiak, J. ; Stepniewska, M. ; Imiolczyk, B. ; Czyrko-Horczak, J. ; Jakubczyk, D. ; Marczak, Ł. ; Plonska-Brzezinska, M. E. (Corresponding author) ; Brzezinski, K. (Corresponding author)Extern*EMBL*

2024
Soc. Cambridge

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Please use a persistent id in citations: doi:10.1039/D4CC03143A

Abstract: We report biochemical and structural studies on inhibiting bacterial S-adenosyl-L-homocysteine hydrolase by transition metal cations. Our results revealed diverse molecular mechanisms of enzyme inactivation. Depending on the cation, the mechanism is based on arresting the enzyme in its closed, inactive conformation, disulfide bond formation within the active site or oxidation of the intermediate form of a cofactor.

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Contributing Institute(s):

1. EMBL-User (EMBL-User)

Research Program(s):

1. 6G3 - PETRA III (DESY) (POF4-6G3) (POF4-6G3)

Experiment(s):

1. PETRA Beamline P13 (PETRA III)

Appears in the scientific report 2024

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Database coverage:
; Chemical Reactions ; Clarivate Analytics Master Journal List ; Current Contents - Physical, Chemical and Earth Sciences ; Ebsco Academic Search ; Essential Science Indicators ; IF < 5 ; Index Chemicus ; JCR ; National-Konsortium ; SCOPUS ; Science Citation Index Expanded ; Web of Science Core Collection

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