KEGG ENZYME: 1.2.3.7

ENZYME: 1.2.3.7

Entry

EC 1.2.3.7                  Enzyme

Name

indole-3-acetaldehyde oxidase;
indoleacetaldehyde oxidase;
IAAld oxidase;
AO1;
indole-3-acetaldehyde:oxygen oxidoreductase

Class

Oxidoreductases;
Acting on the aldehyde or oxo group of donors;
With oxygen as acceptor

Sysname

(indol-3-yl)acetaldehyde:oxygen oxidoreductase

Reaction(IUBMB)

(indol-3-yl)acetaldehyde + H2O + O2 = (indol-3-yl)acetate + H2O2 [RN:R02681]

Reaction(KEGG)

R02681

Substrate

(indol-3-yl)acetaldehyde;
H2O [CPD:C00001];
O2 [CPD:C00007]

Product

(indol-3-yl)acetate [CPD:C00954];
H2O2 [CPD:C00027]

Comment

A hemoprotein. This enzyme is an isoform of aldehyde oxidase (EC 1.2.3.1). It has a preference for aldehydes having an indole-ring structure as substrate [6,7]. It may play a role in plant hormone biosynthesis as its activity is higher in the auxin-overproducing mutant, super-root1, than in wild-type Arabidopsis thaliana [7]. While (indol-3-yl)acetaldehyde is the preferred substrate, it also oxidizes indole-3-carbaldehyde and acetaldehyde, but more slowly. The enzyme from maize contains FAD, iron and molybdenum [4].

History

EC 1.2.3.7 created 1984, modified 2004, modified 2006

Pathway

ec00380

Tryptophan metabolism

ec01100

Metabolic pathways

Orthology

K11817

indole-3-acetaldehyde oxidase

K22417

benzaldehyde dehydrogenase (NAD+) / indole-3-acetaldehyde oxidase

Genes

ATH:	AT1G04580(AO4) AT3G43600(AAO2) AT5G20960(AO1)

ALY:	9310093 9328289

CRB:	17884094 17900582

CSAT:

104706450 104736175 104738981 104762389 104770481 104780236 104790642

EUS:	EUTSA_v10006570mg EUTSA_v10012448mg

BRP:	103844240 103845621 103848036 103851392 103873635

BNA:	106347703 106371001 106371701 106376414 106402186 106406426 106410244 106425715

BOE:	106295510 106317854 106326884 106326885 106335357

RSZ:	108812376 108815136 108832706 108837371 108842248 108861735

THJ:	104799592 104799593

OSA:	4334382 4348072

DOSA:

Os03t0790900-01(Os03g0790900) Os10t0138100-01(Os10g0138100)

OBR:

102704964

OGL:	127765440 127785645

BDI:	100822277 100822898 100836900

ATS:	109747740 109747741 109747742 109752661 109765340

TDC:	119303471 119303472 119303473 119303474 119303476 119303477 119312128 119312132 119345299

TAES:

123105337 123105340 123105341 123105342 123105343 123105344 123113606 123113607 123113609 123123127 123123129 123123132 123123133

TUA:	125510893 125510896 125510934 125546255

LPER:

127292476 127293769 127293770 127314462

LRD:	124685088 124690068 124703720 124704526

SBI:	8061191 8084125 8084128

ZMA:	103644157 542228 542229

SITA:

101754702 101755113 101756196 101764191

SVS:	117838077 117838078 117839666

PVIR:

120649504 120649505 120691959 120693301

PHAI:

112878335

ZOF:	122001229 122005521 122008453 122014832 122014905 122014911 122046391 122046414

» show all

Reference

1 [PMID:16660220]

Authors

Bower PJ, Brown HM, Purves WK.

Title

Cucumber Seedling Indoleacetaldehyde Oxidase.

Journal

Plant Physiol 61:107-110 (1978)
DOI:10.1104/pp.61.1.107

Reference

Authors

Miyata, S., Suzuki, Y., Kamisaka, S. and Masuda, Y.

Title

Indole-3-acetaldehyde oxidase of pea-seedlings.

Journal

Physiol Plant 51:402-406 (1981)

Reference

Authors

Rajagopal, R.

Title

Metabolism of indole-3-acetaldehyde. III. Some characteristics of the aldehyde oxidase of Avena coleoptiles.

Journal

Physiol Plant 24:272-281 (1971)

Reference

4 [PMID:12226218]

Authors

Koshiba T, Saito E, Ono N, Yamamoto N, Sato M

Title

Purification and Properties of Flavin- and Molybdenum-Containing Aldehyde Oxidase from Coleoptiles of Maize.

Journal

Plant Physiol 110:781-789 (1996)
DOI:10.1104/pp.110.3.781

Sequence

[zma:542228]

Reference

5 [PMID:12231908]

Authors

Koshiba T, Matsuyama H.

Title

An in Vitro System of Indole-3-Acetic Acid Formation from Tryptophan in Maize (Zea mays) Coleoptile Extracts.

Journal

Plant Physiol 102:1319-1324 (1993)
DOI:10.1104/pp.102.4.1319

Reference

6 [PMID:9615466]

Authors

Sekimoto H, Seo M, Kawakami N, Komano T, Desloire S, Liotenberg S, Marion-Poll A, Caboche M, Kamiya Y, Koshiba T

Title

Molecular cloning and characterization of aldehyde oxidases in Arabidopsis thaliana.

Journal

Plant Cell Physiol 39:433-42 (1998)
DOI:10.1093/oxfordjournals.pcp.a029387

Sequence

[ath:AT5G20960 AT3G43600]

Reference

7 [PMID:9489015]

Authors

Seo M, Akaba S, Oritani T, Delarue M, Bellini C, Caboche M, Koshiba T.

Title

Higher activity of an aldehyde oxidase in the auxin-overproducing superroot1 mutant of Arabidopsis thaliana.

Journal

Plant Physiol 116:687-93 (1998)
DOI:10.1104/pp.116.2.687

Sequence

[ath:AT5G20960]

Other DBs

ExplorEnz - The Enzyme Database:

1.2.3.7

IUBMB Enzyme Nomenclature:

1.2.3.7

ExPASy - ENZYME nomenclature database:

1.2.3.7

BRENDA, the Enzyme Database:

1.2.3.7

CAS:	66082-22-2

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