Results 21 to 30 of about 660,873 (335)

The Substrate Specificity of Fumarase

open access: yesJournal of Biological Chemistry, 1968
Abstract The substrate specificity of fumarase has been studied by measuring the ability of the enzyme to hydrate or dehydrate derivatives of fumarate and l-malate. Fumarase was observed to hydrate fumarate and its derivatives in the order, fluorofumarate g fumarate g chlorofumarate g bromofumarate g acetylenedicarboxylate g iodofumarate g mesaconate ...
G M Hass, Robert L. Hill, John W. Teipel
openaire   +3 more sources

Dissecting the Cytochrome P450 OleP Substrate Specificity: Evidence for a Preferential Substrate

open access: yesBiomolecules, 2020
The cytochrome P450 OleP catalyzes the epoxidation of aliphatic carbons on both the aglycone 8.8a-deoxyoleandolide (DEO) and the monoglycosylated L-olivosyl-8.8a-deoxyoleandolide (L-O-DEO) intermediates of oleandomycin biosynthesis.
Giacomo Parisi   +10 more
doaj   +1 more source

Structure-based engineering of substrate specificity for pinoresinol-lariciresinol reductases

open access: yesNature Communications, 2021
Pinoresinol–lariciresinol reductases (PLRs) are enzymes involved in the lignan biosynthesis. Here, crystal structures of three PLRs in the apo, substrate-bound and product-bound states, and accompanying mutagenesis provide insight into PLRs catalytic ...
Ying Xiao   +13 more
doaj   +1 more source

Crystal Structure and Substrate Specificity of PTPN12

open access: yesCell Reports, 2016
PTPN12 is an important tumor suppressor that plays critical roles in various physiological processes. However, the molecular basis underlying the substrate specificity of PTPN12 remains uncertain.
Hui Li   +18 more
doaj   +1 more source

Oscillation-like diffusion of two-dimensional liquid dusty plasmas on one-dimensional periodic substrates with varied widths [PDF]

open access: yesPhysics of Plasmas 27, 033702 (2020), 2020
The long-time diffusion of two-dimensional dusty plasmas on a one-dimensional periodic substrate with varied widths is investigated using Langevin dynamical simulations. When the substrate is narrow and the dust particles form a single row, the diffusion is the smallest in both directions.
arxiv   +1 more source

Substrate specificity of human MCPIP1 endoribonuclease

open access: yesScientific Reports, 2018
MCPIP1, also known as Regnase-1, is a ribonuclease crucial for regulation of stability of transcripts related to inflammatory processes. Here, we report that MCPIP1 acts as an endonuclease by degrading several stem-loop RNA structures and single-stranded
Mateusz Wilamowski   +3 more
doaj   +1 more source

Insights into a Cancer-Target Demethylase: Substrate Prediction through Systematic Specificity Analysis for KDM3A

open access: yesBiomolecules, 2022
Jumonji C (JmjC) lysine demethylases (KDMs) catalyze the removal of methyl (-CH3) groups from modified lysyl residues. Several JmjC KDMs promote cancerous properties and these findings have primarily been in relation to histone demethylation.
Anand Chopra   +2 more
doaj   +1 more source

Comparative Studies on Retroviral Proteases: Substrate Specificity

open access: yesViruses, 2010
Exogenous retroviruses are subclassified into seven genera and include viruses that cause diseases in humans. The viral Gag and Gag-Pro-Pol polyproteins are processed by the retroviral protease in the last stage of replication and inhibitors of the HIV-1
József Tözsér
doaj   +1 more source

Elucidation of substrate specificity in Aspergillus nidulans UDP-galactose-4-epimerase. [PDF]

open access: yesPLoS ONE, 2013
The frequency of invasive fungal infections has rapidly increased in recent years. Current clinical treatments are experiencing decreased potency due to severe host toxicity and the emergence of fungal drug resistance.
Sean A Dalrymple   +4 more
doaj   +1 more source

Substrate Specificity of Chlorophyllase [PDF]

open access: yesPlant Physiology, 1975
Apparent Km and V(max) values were obtained for hydrolysis of methyl and ethyl chlorophyllides a, methyl and ethyl pheophorbide a, and 9-hydroxymethyl pheophorbide a by chlorophyllase from Ailanthus altissima. Analysis of substrate specificity data for chlorophyllase indicates that the presence of a 9-keto group and a methyl alcohol group esterified at
openaire   +3 more sources

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