関: 15-lipoxygenase

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/08/02 19:53:00」(JST)

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In enzymology, an arachidonate 15-lipoxygenase (EC 1.13.11.33) is an enzyme that catalyzes the chemical reaction

arachidonate + O₂ (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate

Thus, the two substrates of this enzyme are arachidonate and O₂, whereas its product is (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate.

This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O₂ as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O₂. The systematic name of this enzyme class is arachidonate:oxygen 15-oxidoreductase. Other names in common use include 15-lipoxygenase, linoleic acid omega6-lipoxygenase, and omega6 lipoxygenase. This enzyme participates in arachidonic acid metabolism and linoleic acid metabolism.

Structural studies[edit source | edit]

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1LOX.

References[edit source | edit]

Bryant RW, Bailey JM, Schewe T, Rapoport SM (1982). "Positional specificity of a reticulocyte lipoxygenase. Conversion of arachidonic acid to 15-S-hydroperoxy-eicosatetraenoic acid". J. Biol. Chem. 257 (11): 6050–5. PMID 6804460.
Narumiya S, Salmon JA (1982). "Arachidonic acid-15-lipoxygenase from rabbit peritoneal polymorphonuclear leukocytes". Methods' Enzymol. Methods in Enzymology 86: 45–8. doi:10.1016/0076-6879(82)86166-1. ISBN 978-0-12-181986-6. PMID 6813644.
Oliw EH, Sprecher H (1989). "Metabolism of polyunsaturated fatty acids by an (n - 6)-lipoxygenase associated with human ejaculates". Biochim. Biophys. Acta. 1002 (3): 283–91. PMID 2496760.
B; Steczko, J; Dixon, JE; Hermodson, M; Yazdanparast, R; Axelrod, B (1987). "Primary structure of soybean lipoxygenase-1". J. Biol. Chem. 262 (21): 10080–5. PMID 3112136.

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English Journal

Arachidonate 12/15-Lipoxygenase-Induced Inflammation and Oxidative Stress Are Involved in the Development of Diabetic Cardiomyopathy.

Suzuki H1, Kayama Y2, Sakamoto M1, Iuchi H1, Shimizu I3, Yoshino T4, Katoh D4, Nagoshi T4, Tojo K1, Minamino T5, Yoshimura M4, Utsunomiya K1.
Diabetes.Diabetes.2014 Sep 3. pii: DB_131896. [Epub ahead of print]
Diabetes affects cardiac structure and function, and it has been suggested that diabetes leads to cardiomyopathy. Arachidonate 12/15 lipoxygenase (LOX) has been suggested to play an important role in atherogenesis and heart failure. However, the role of 12/15-LOX in diabetic cardiomyopathy has not b
PMID 25187369

Arachidonate 15-lipoxygenase is required for chronic myeloid leukemia stem cell survival.

Chen Y, Peng C, Abraham SA, Shan Y, Guo Z, Desouza N, Cheloni G, Li D, Holyoake TL, Li S.
The Journal of clinical investigation.J Clin Invest.2014 Sep 2;124(9):3847-62. doi: 10.1172/JCI66129. Epub 2014 Aug 8.
Cancer stem cells (CSCs) are responsible for the initiation and maintenance of some types of cancer, suggesting that inhibition of these cells may limit disease progression and relapse. Unfortunately, few CSC-specific genes have been identified. Here, we determined that the gene encoding arachidonat
PMID 25105362

Kinetic investigation of the rate-limiting step of manganese- and iron-lipoxygenases.

Wennman A1, Karkehabadi S1, Oliw EH2.
Archives of biochemistry and biophysics.Arch Biochem Biophys.2014 Aug;555-556:9-15. doi: 10.1016/j.abb.2014.05.014. Epub 2014 May 21.
Lipoxygenases (LOX) oxidize polyunsaturated fatty acids to hydroperoxides, which are generated by proton coupled electron transfer to the metal center with FeIIIOH- or MnIIIOH-. Hydrogen abstraction by FeIIIOH- of soybean LOX-1 (sLOX-1) is associated with a large deuterium kinetic isotope effect (D-
PMID 24857825

Japanese Journal

ニジマス白血球のアラキドン酸15-リポキシゲナーゼの精製とその諸性質

吉田美夫,沖増英治,雨村明倫,ヨシダヨシオ,オキマスエイジ,アメムラアキノリ,Yoshio Yoshida,Eiji Okimasu,Akinori Amemura
福山大学附属内海生物資源研究所報告 4, 1-12, 1993-12
… ニジマス白血球の15-LO酵素の分子量は約70,000であり,哺乳類の15-LO酵素の分子量とも類似していた。 … しかし,至適反応温度は15℃であり,これは至適反応温度を高温領域にもつ哺乳類とは異なっていた。 … ニジマス白血球の15-LO酵素の最終精製段階における回収率は3.1%,精製純度が4.8倍と非常に不安定な酵素であることが明らかになった。 …
NAID 120005500038

ニジマス白血球のアラキドン酸15-リポキシゲナーゼの精製とその諸性質

吉田美夫,沖増英治,雨村明倫
福山大学附属内海生物資源研究所報告 4, 1-12, 1993-12
… ニジマス白血球の15-LO酵素の分子量は約70,000であり,哺乳類の15-LO酵素の分子量とも類似していた。 … しかし,至適反応温度は15℃であり,これは至適反応温度を高温領域にもつ哺乳類とは異なっていた。 … ニジマス白血球の15-LO酵素の最終精製段階における回収率は3.1%,精製純度が4.8倍と非常に不安定な酵素であることが明らかになった。 …
NAID 110007407976

アラキドン酸12-リポキシゲナーゼの生化学的ならびに分子生物学的研究

高橋吉孝 [他],鈴木啓史,荒川俊哉,吉本谷博,山本尚三
ビタミン 67(1), 1-16, 1993-01-25
… Arachidonate 12-lipoxygenase is a dioxygenase which incorporates one molecule of oxygen into arachidonic acid and produces 12S-hydroperoxy-5, 8, 10, 14-eicosate-traenoic acid. … Two types of 12-lipoxygenase are distinguishable in terms of substrate specificity. …
NAID 110002844276

「アラキドン酸15-リポキシゲナーゼ」

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arachidonate 15-lipoxygenase
Identifiers
EC number	1.13.11.33
CAS number	82249-77-2
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
Search
PMC	articles
PubMed	articles
NCBI	proteins