L-amino-acid oxidase: Difference between revisions
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{{Short description| | {{Short description|Enzyme that catalyzes the oxidative deamination of L-amino acids}} | ||
{{DISPLAYTITLE:L-amino-acid oxidase}} | |||
'''L-amino acid oxidase''' (LAAO) is a [[ | ==L-amino-acid oxidase== | ||
[[File:3kve.jpg|thumb|right|Crystal structure of L-amino-acid oxidase]] | |||
'''L-amino-acid oxidase''' (LAAO) is a [[flavoprotein]] enzyme that catalyzes the oxidative deamination of [[L-amino acids]] to produce the corresponding [[α-keto acids]], [[ammonia]], and [[hydrogen peroxide]]. This enzyme is found in various organisms, including [[snake venom]]s, where it plays a role in the digestion of prey and defense mechanisms. | |||
==Structure | ==Structure== | ||
L-amino acid oxidase is a | L-amino-acid oxidase is a dimeric enzyme, with each subunit containing a [[flavin adenine dinucleotide]] (FAD) cofactor. The enzyme's active site is responsible for binding the L-amino acid substrate and facilitating the redox reaction. The crystal structure of LAAO reveals a complex arrangement of alpha helices and beta sheets that form the overall three-dimensional structure of the enzyme. | ||
The | ==Mechanism of Action== | ||
[[File:LAAOwithLalaninerxn.png|thumb|left|Reaction of L-amino-acid oxidase with L-alanine]] | |||
The mechanism of L-amino-acid oxidase involves the initial binding of the L-amino acid substrate to the active site. The FAD cofactor accepts electrons from the substrate, leading to the formation of an imino acid intermediate. This intermediate is then hydrolyzed to produce the corresponding α-keto acid and ammonia. The reduced FAD is reoxidized by molecular oxygen, generating hydrogen peroxide as a byproduct. | |||
==Biological Function== | |||
L-amino-acid oxidase is involved in various biological processes, including the catabolism of amino acids and the production of reactive oxygen species. In snake venoms, LAAO contributes to the toxicity by generating hydrogen peroxide, which can cause oxidative damage to tissues. Additionally, the enzyme's ability to produce ammonia and α-keto acids plays a role in the digestion of prey. | |||
==Applications== | |||
L-amino-acid oxidase has potential applications in biotechnology and medicine. Its ability to produce hydrogen peroxide can be harnessed for antimicrobial purposes. Furthermore, the enzyme's specificity for L-amino acids makes it a useful tool in analytical biochemistry for the determination of amino acid concentrations. | |||
== | |||
L-amino acid oxidase | |||
== | ==Reaction Scheme== | ||
[[File:LAAOreactionscheme.png|thumb|right|Reaction scheme of L-amino-acid oxidase]] | |||
The overall reaction catalyzed by L-amino-acid oxidase can be summarized as follows: | |||
:L-amino acid + O₂ → α-keto acid + NH₃ + H₂O₂ | |||
L-amino acid | |||
This reaction highlights the enzyme's role in oxidative deamination and the production of reactive oxygen species. | |||
==Related pages== | |||
* [[Flavoprotein]] | |||
==Related | * [[Oxidative deamination]] | ||
* [[ | * [[Snake venom]] | ||
* [[ | |||
* [[Reactive oxygen species]] | * [[Reactive oxygen species]] | ||
[[Category:Enzymes]] | [[Category:Enzymes]] | ||
[[Category:Flavoproteins]] | |||
[[Category:Oxidoreductases]] | [[Category:Oxidoreductases]] | ||
Latest revision as of 14:23, 21 February 2025
Enzyme that catalyzes the oxidative deamination of L-amino acids
L-amino-acid oxidase[edit]
L-amino-acid oxidase (LAAO) is a flavoprotein enzyme that catalyzes the oxidative deamination of L-amino acids to produce the corresponding α-keto acids, ammonia, and hydrogen peroxide. This enzyme is found in various organisms, including snake venoms, where it plays a role in the digestion of prey and defense mechanisms.
Structure[edit]
L-amino-acid oxidase is a dimeric enzyme, with each subunit containing a flavin adenine dinucleotide (FAD) cofactor. The enzyme's active site is responsible for binding the L-amino acid substrate and facilitating the redox reaction. The crystal structure of LAAO reveals a complex arrangement of alpha helices and beta sheets that form the overall three-dimensional structure of the enzyme.
Mechanism of Action[edit]
The mechanism of L-amino-acid oxidase involves the initial binding of the L-amino acid substrate to the active site. The FAD cofactor accepts electrons from the substrate, leading to the formation of an imino acid intermediate. This intermediate is then hydrolyzed to produce the corresponding α-keto acid and ammonia. The reduced FAD is reoxidized by molecular oxygen, generating hydrogen peroxide as a byproduct.
Biological Function[edit]
L-amino-acid oxidase is involved in various biological processes, including the catabolism of amino acids and the production of reactive oxygen species. In snake venoms, LAAO contributes to the toxicity by generating hydrogen peroxide, which can cause oxidative damage to tissues. Additionally, the enzyme's ability to produce ammonia and α-keto acids plays a role in the digestion of prey.
Applications[edit]
L-amino-acid oxidase has potential applications in biotechnology and medicine. Its ability to produce hydrogen peroxide can be harnessed for antimicrobial purposes. Furthermore, the enzyme's specificity for L-amino acids makes it a useful tool in analytical biochemistry for the determination of amino acid concentrations.
Reaction Scheme[edit]
The overall reaction catalyzed by L-amino-acid oxidase can be summarized as follows:
- L-amino acid + O₂ → α-keto acid + NH₃ + H₂O₂
This reaction highlights the enzyme's role in oxidative deamination and the production of reactive oxygen species.
