ジアミンオキシダーゼ

識別子
EC番号1.4.3.22
データベース
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAM ⇒profile
PDB構造RCSB PDB PDBj PDBe PDBsum
遺伝子オントロジー ⇒AmiGO / QuickGO

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ジアミンオキシダーゼ(diamine oxidase)は、アルギニン、プロリン、ヒスチジン、トリプトファン代謝酵素の一つで、次の化学反応を触媒する酸化還元酵素である。ヒスタミン + H2O + O2 ⇌ {\displaystyle \rightleftharpoons } (イミダゾール-4-イル)アセトアルデヒド + NH3 + H2O2

反応式の通り、この酵素の基質はヒスタミンとH2OとO2、生成物は(イミダゾール-4-イル)アセトアルデヒドとNH3とH2O2である。

組織名はhistamine:oxygen oxidoreductase (deaminating)で、別名にamine oxidase (ambiguous); amine oxidase (copper-containing) (ambiguous); CAO (ambiguous); Cu-containing amine oxidase (ambiguous); copper amine oxidase (ambiguous); diamine oxidase (ambiguous); diamino oxhydrase (ambiguous); histaminase; histamine deaminase (incorrect); semicarbazide-sensitive amine oxidase (incorrect); SSAO (incorrect)がある。
参考文献

Zeller, E.A. Diamine oxidases. In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds), The Enzymes, 2nd edn, vol. 8, Academic Press, New York, 1963, pp. 313-335.

Crabbe, M.J., Waight, R.D., Bardsley, W.G., Barker, R.W., Kelly, I.D. and Knowles, P.F. (1976). “Human placental diamine oxidase. Improved purification and characterization of a copper- and manganese-containing amine oxidase with novel substrate specificity.”. Biochem. J. 155: 679-687. .mw-parser-output cite.citation{font-style:inherit;word-wrap:break-word}.mw-parser-output .citation q{quotes:"\"""\"""'""'"}.mw-parser-output .citation.cs-ja1 q,.mw-parser-output .citation.cs-ja2 q{quotes:"「""」""『""』"}.mw-parser-output .citation:target{background-color:rgba(0,127,255,0.133)}.mw-parser-output .id-lock-free a,.mw-parser-output .citation .cs1-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/6/65/Lock-green.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-limited a,.mw-parser-output .id-lock-registration a,.mw-parser-output .citation .cs1-lock-limited a,.mw-parser-output .citation .cs1-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/d/d6/Lock-gray-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-subscription a,.mw-parser-output .citation .cs1-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/a/aa/Lock-red-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .cs1-ws-icon a{background:url("//upload.wikimedia.org/wikipedia/commons/4/4c/Wikisource-logo.svg")right 0.1em center/12px no-repeat}.mw-parser-output .cs1-code{color:inherit;background:inherit;border:none;padding:inherit}.mw-parser-output .cs1-hidden-error{display:none;color:#d33}.mw-parser-output .cs1-visible-error{color:#d33}.mw-parser-output .cs1-maint{display:none;color:#3a3;margin-left:0.3em}.mw-parser-output .cs1-format{font-size:95%}.mw-parser-output .cs1-kern-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right{padding-right:0.2em}.mw-parser-output .citation .mw-selflink{font-weight:inherit}PMID 182134. 

Chassande, O., Renard, S., Barbry, P. and Lazdunski, M. (1994). “The human gene for diamine oxidase, an amiloride binding protein. Molecular cloning, sequencing, and characterization of the promoter.”. J. Biol. Chem. 269: 14484-14489. PMID 8182053. 

Houen, G. (1999). “Mammalian Cu-containing amine oxidases (CAOs): new methods of analysis, structural relationships, and possible functions.”. APMIS Suppl. 96: 1-46. PMID 10668504. 

Elmore, B.O., Bollinger, J.A. and Dooley, D.M. (2002). “Human kidney diamine oxidase: heterologous expression, purification, and characterization.”. J. Biol. Inorg. Chem. 7: 565-579. PMID 12072962.