Results 11 to 20 of about 195,221 (99)

Contribution of aldehyde oxidase, xanthine oxidase and aldehyde dehydro-genase on the oxidation of aromatic aldehydes

open access: yesChemical Research in Toxicology, 2004
NoAliphatic aldehydes have a high affinity toward aldehyde dehydrogenase activity but are relatively poor substrates of aldehyde oxidase and xanthine oxidase.
Panoutsopoulos, Georgios I.   +4 more
core   +5 more sources

Metabolism of isovanillin by aldehyde oxidase, xanthine oxidase, aldehyde dehydrogenase and liver slices.

open access: yesPharmacology, 2005
NoAromatic aldehydes are good substrates of aldehyde dehydrogenase activity but are relatively poor substrates of aldehyde oxidase and xanthine oxidase.
Panoutsopoulos, Georgios I.   +3 more
core   +4 more sources

Studies on the Mechanism of Aldehyde Oxidase and Xanthine Oxidase [PDF]

open access: yesThe Journal of Organic Chemistry, 2008
DFT calculations support a concerted mechanism for xanthine oxidase and aldehyde oxidase hydride displacement from the sp(2) carbon of 6-substituted 4-quinazolinones. The variations in transition state structure show that C-O bond formation is nearly complete in the transition state and the transition state changes are anti-Hammond with the C-H and C-O
ALFARO, Joshua F, JONES, Jeffrey P
openaire   +3 more sources

Drosophila Melanogaster as a Model for Molybdo-Flavoenzyme Mediated Protection against Chemical and Physical Stress [PDF]

open access: yes
Aldehyde oxidase (AO) and xanthine oxidoreductase (XOR) are molybdo-flavoenzymes (MFEs) involved in the oxidation of hundreds of endogenous and exogenous aldehydes and N-heterocyclic compounds many of which are drugs, vitamins and environmental ...
Al Salhen, Khaled S
core   +3 more sources

Involvement of aldehyde oxidase in the metabolism of aromatic and aliphatic aldehyde-odorants in the mouse olfactory epithelium

open access: yes, 2022
Xenobiotic-metabolizing enzymes (XMEs) expressed in the olfactory epithelium (OE) are known to metabolize odorants. Aldehyde oxidase (AOX) recognizes a wide range of substrates among which are substrates with aldehyde groups. Some of these AOX substrates
Sanoh, Seigo   +17 more
core   +1 more source

Research progress of aldehyde oxidases in plants

open access: yesPeerJ, 2022
Plant aldehyde oxidases (AOs) are multi-functional enzymes, and they could oxidize abscisic aldehyde into ABA (abscisic acid) or indole acetaldehyde into IAA (indoleacetic acid) as the last step, respectively. AOs can be divided into four groups based on their biochemical and physiological functions.
Jun Wu   +4 more
openaire   +3 more sources

Aldehyde oxidase 1 gene is regulated by Nrf2 pathway [PDF]

open access: yes, 2012
Aldehyde oxidase is a member of the molybd-flavo enzyme family that catalyzes the hydroxylation of heterocycles and the oxidation of aldehydes into corresponding carboxylic acids.
Ohno, Takashi   +5 more
core   +1 more source

Role of Fish Hepatic Aldehyde Oxidase in Oxidative in vitro Metabolism of Phenanthridine Heterocyclic Aromatic Compound

open access: yes, 2014
Aldehyde oxidase is molybdo-flavoenzyme involved in the oxidation of hundreds of endogenous and exogenous and N-heterocyclic compounds and environmental pollutants.
Khaled S. Al Salhen
core   +1 more source

The mammalian aldehyde oxidase gene family [PDF]

open access: yesHuman Genomics, 2009
Aldehyde oxidases (EC 1.2.3.1) are a small group of structurally conserved cytosolic proteins represented in both the animal and plant kingdoms. In vertebrates, aldehyde oxidases constitute the small sub-family of molybdo-flavoenzymes, along with the evolutionarily and structurally related protein, xanthine oxidoreductase.
Garattini Enrico   +2 more
openaire   +3 more sources

Metabolism of cryptolepine and 2-fluorocryptolepine by aldehyde oxidase

open access: yes, 2011
NoObjectives To investigate the metabolism of cryptolepine and some cryptolepine analogues by aldehyde oxidase, and to assess the implications of the results on the potential of cryptolepine analogues as antimalarial agents.
Wheelhouse, Richard T.   +5 more
core   +1 more source

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