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Literature summary for 2.3.1.72 extracted from

  • Kowalczyk, S.; Jakubowska, A.; Zielinska, E.; Bandurski, R.S.
    Bifunctional indole-3-acetyl transferase catalyses synthesis and hydrolysis of indole-3-acetyl-myo-inositol in immature endosperm of Zea mays (2003), Physiol. Plant., 119, 165-174.
No PubMed abstract available
Search for more literature for 2.3.1.72

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
654000
-
 1 * 654000, enzyme exists as both a monomeric and homo- or heterodimeric form, SDS-PAGE Zea mays

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
indole-3-acetyl-beta-1-D-glucoside + myo-inositol Zea mays
-
 D-glucose + indole-3-acetyl-myo-inositol
-
 ?

Organism

Organism UniProt Comment Textmining
Zea mays
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein polypeptides of 56400 Da and 53500 Da have the same primary structure and the 3000 Da difference in molecular mass is probably caused by different glycosylation levels Zea mays

Purification (Commentary)

Purification (Comment) Organism
-
 Zea mays

Source Tissue

Source Tissue Comment Organism Textmining
endosperm immature Zea mays
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
indole-3-acetyl-beta-1-D-glucoside + myo-inositol
-
 Zea mays D-glucose + indole-3-acetyl-myo-inositol
-
 ?

Subunits

Subunits Comment Organism
dimer enzyme exists as both a monomeric and homo- or heterodimeric form Zea mays
monomer 1 * 654000, enzyme exists as both a monomeric and homo- or heterodimeric form, SDS-PAGE Zea mays

Synonyms

Synonyms Comment Organism
1-O-(indole-3-acetyl)-beta-D-glucose:myo-inositol indoleacetyl transferase
-
 Zea mays
IA-myo-inositol synthase
-
 Zea mays
Ialnos synthase
-
 Zea mays