酸化的脱アミノ

WordNet

removal of the amino radical from an amino acid or other amino compound (同)deaminization
taking place in the presence of oxygen; "oxidative glycolysis"; "oxidative rancidity"

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2017/10/23 01:54:34」(JST)

wiki en

Oxidative deamination is a form of deamination that generates α-keto acids and other oxidized products from amine-containing compounds, and occurs largely in the liver and kidney. Oxidative deamination is an important step in the catabolism of amino acids, generating a more metabolizable form of the amino acid, and also generating ammonia as a toxic byproduct. The ammonia generated in this process can then be neutralized into urea via the urea cycle.

Much of the oxidative deamination occurring in cells involves the amino acid glutamate, which can be oxidatively deaminated by the enzyme glutamate dehydrogenase (GDH), using NAD or NADP as a coenzyme. This reaction generates α-ketoglutarate (α-KG) and ammonia. Glutamate can then be regenerated from α-KG via the action of transaminases, which catalyze the transfer of an amino group from an amino acid to an α-keto acid. In this manner, an amino acid can transfer its amine group to glutamate, after which GDH can then liberate ammonia via oxidative deamination. This is a common pathway during amino acid catabolism.^[1]

Another enzyme responsible for oxidative deamination is monoamine oxidase, which catalyzes the deamination of monoamines via addition of oxygen. This generates the corresponding ketone- or aldehyde-containing form of the molecule, and generates ammonia. Monoamine oxidases MAO-A and MAO-B play vital roles in the degradation and inactivation of monoamine neurotransmitters such as serotonin and epinephrine.^[2] Monoamine oxidases are important drug targets, targeted by MAO inhibitors (MAOIs) such as selegiline.

References

^ "Amino Acid Catabolism: Nitrogen". Rensselaer Polytechnic Institute. Retrieved 20 June 2017.
^ Edmondson DE, Mattevi A, Binda C, Li M, Hubálek F (August 2004). "Structure and mechanism of monoamine oxidase". Current Medicinal Chemistry. 11 (15): 1983–93. PMID 15279562. doi:10.2174/0929867043364784.

External links

Diagram from Elmhurst

This biochemistry article is a stub. You can help Wikipedia by expanding it.

UpToDate Contents

全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.

1. 心不全における酸化ストレスの役割 role of oxidative stress in heart failure
2. 成人におけるうつ病治療としてのモノアミン酸化酵素阻害剤（MAOI） monoamine oxidase inhibitors maois for treating depressed adults
3. 高二酸化炭素血症の許容（Permissive hypercapnia） permissive hypercapnia
4. 家族性筋萎縮性側索硬化症 familial amyotrophic lateral sclerosis
5. 薬物および毒素による外因性非自己免疫性溶血性貧血 extrinsic nonautoimmune hemolytic anemia due to drugs and toxins

English Journal

Cytotoxicity and inhibition of platelet aggregation caused by an l-amino acid oxidase from Bothrops leucurus venom.

Naumann GB, Silva LF, Silva L, Faria G, Richardson M, Evangelista K, Kohlhoff M, Gontijo CM, Navdaev A, de Rezende FF, Eble JA, Sanchez EF.SourceResearch and Development Center, Ezequiel Dias Foundation, 30510-0103, Belo Horizonte, Brazil.
Biochimica et biophysica acta.Biochim Biophys Acta.2011 Jul;1810(7):683-94. Epub 2011 Apr 22.
BACKGROUND: Multifunctional l-amino acid oxidases (LAAOs) occur widely in snake venoms.METHODS: The l-AAO from Bothrops leucurus (Bl-LAAO) venom was purified using a combination of molecular exclusion and ion-exchange chromatographies. We report some biochemical features of Bl-LAAO associated with i
PMID 21539897

From caffeine to fish waste: amine compounds present in food and drugs and their interactions with primary amine oxidase.

Olivieri A, Rico D, Khiari Z, Henehan G, O'Sullivan J, Tipton K.SourceSchool of Biochemistry and Immunology, Trinity College, Dublin 2, Ireland, oliviera@tcd.ie.
Journal of neural transmission (Vienna, Austria : 1996).J Neural Transm.2011 Jul;118(7):1079-89. Epub 2011 Mar 4.
Tissue bound primary amine oxidase (PrAO) and its circulating plasma-soluble form are involved, through their catalytic activity, in important cellular roles, including the adhesion of lymphocytes to endothelial cells during various inflammatory conditions, the regulation of cell growth and maturati
PMID 21373760

Japanese Journal

The Silent Form of Quinohemoprotein Amine Dehydrogenase from Paracoccus denitrificans

FUJIEDA Nobutaka,MORI Megumi,IKEDA Tokuji,KANO Kenji
Bioscience, Biotechnology, and Biochemistry 73(3), 524-529, 2009
… Quinohemoprotein amine dehydrogenase (QH-AmDH) from Paracoccus denitrificans is an αβγ heterotrimeric enzyme catalyzing oxidative deamination of amines with large substitutes, such as butylamine and benzylamine. …
NAID 130000407504

細胞外マトリックスタンパク質の架橋構造と生成機構 : とくにコラーゲンとエラスチンについて

須山享三
仙台大学紀要 39(2), 145-160, 2008-03
… The basic mechanism of cross-linking is oxidative deamination of the ε-amino groups in lysine or hydroxylysine residues, catalyzed by lysyl oxidase. … It is believed that oxidative deamination is the only step in cross-link formation that is catalyzed enzymatically. …
NAID 110007147948