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Showing results 1 to 4 of 4

Journal Article

An Atypical E3 Ligase Module in UBR4 Mediates Destabilization of N-degron Substrates

Authors : Greer, Lucy Barnsby (2023)

UBR4 is an E3 ligase (E3) of the N-degron pathway and is involved in neurodevelopment, age-associated muscular atrophy and cancer progression. The location and mechanistic classification of the E3 module within the 600 kDa protein UBR4 remains unknown. Herein, we identify and characterize, at a biochemical and structural level, a distinct E3 module within human UBR4 consisting of a novel “hemiRING” zinc finger, a helical-rich UBR Zinc-finger Interacting&...

Journal article

Direct Estimate of the Specificity Constant: A Possibility or a Fluke? Pre-steady-state Substrate Concentrations and Enabling Mathematical Equations

Authors : Udema, Ikechukwu Iloh (2023)

A high-ranking scientist has recently proposed the need for direct estimation of the specificity constant rather than by calculation after a separate determination of maximum velocity and the Michaelis-Menten constant (KM). The objectives of this study are to derive novel equations for the zero-arbitrary determination of pre-steady-state (PSS) concentration of the substrate suitable for PSS assays, direct estimation of specificity constant (SC) under ...

Journal article

Etmopterus lantern sharks use coelenterazine as the substrate for their luciferin-luciferase bioluminescence system

Authors : Mizuno, Gaku (2021)

The lantern shark genus Etmopterus is a group of deep-sea bioluminescent fishes. Theyemit blue light mainly from the ventral body surface, and the primary biological functionis considered to be for camouflage by counterillumination. In this study, we detected bothcoelenterazine and coelenterazine-specific luciferase activity in the ventral photophoretissues. The results suggested that bioluminescence in lantern sharks is produced usingcoelenterazine as the substrate for the ...

Journal article

The human GID complex engages two independent modules for substrate recruitment

Authors : Mohamed, Weaam I. (2021)

The human GID (hGID) complex is an evolutionary conserved E3 ubiquitin ligase regulating diverse biological processes including glucose metabolism and cell cycle progression. However, the biochemical function and substrate recognition of the multi-subunit complex remains poorly understood. While the yeast GID complex recognizes Pro/N-end rule substrates via yeast Gid4, the human GID complex requires a WDR26/Gid7-dependent module to trigger proteasomal&#x...