Information on EC 2.3.1.72 - indoleacetylglucose-inositol O-acyltransferase

487444, 487445

Substrates: i.e. 1-O-indol-3-yl-acetyl-beta-D-glucose, high specificity
Products: -

indole-3-acetyl-beta-1-D-glucoside + myo-inositol

D-glucose + indole-3-acetyl-myo-inositol

Substrates: scyllo-inositol or myo-inosose-2 can replace myo-inositol
Products: -

indole-3-acetyl-beta-1-D-glucoside + myo-inositol

D-glucose + indole-3-acetyl-myo-inositol

Substrates: myo-inositol-D-galactopyranose, cyclohexanol, mannitol, glycerol
Products: -

indole-3-acetyl-beta-1-D-glucoside + myo-inositol

D-glucose + indole-3-acetyl-myo-inositol

Substrates: involved in biosynthesis of indole-3-acetyl-beta-1,4-glucan
Products: -

indole-3-acetyl-beta-1-D-glucoside + myo-inositol

D-glucose + indole-3-acetyl-myo-inositol

Substrates: -
Products: -

show all columns Go to Natural Substrate Search

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

LITERATURE

COMMENTARY

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

1-O-(indol-3-yl)acetyl-beta-D-glucose + myo-inositol

D-glucose + O-(indol-3-yl)acetyl-myo-inositol

Substrates: -
Products: -

indole-3-acetyl-beta-1-D-glucoside + myo-inositol

D-glucose + indole-3-acetyl-myo-inositol

indole-3-acetyl-beta-1-D-glucoside + myo-inositol

D-glucose + indole-3-acetyl-myo-inositol

Substrates: involved in biosynthesis of indole-3-acetyl-beta-1,4-glucan
Products: -

indole-3-acetyl-beta-1-D-glucoside + myo-inositol

D-glucose + indole-3-acetyl-myo-inositol

Substrates: -
Products: -

show all columns Go to Inhibitor Search

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INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

2-mercaptoethanol

74% inhibition at 5 mM

Dithionite

inhibition at 40 mM

dithiothreitol

98% inhibition at 5 mM

phenylmethylsulfonyl fluoride

show all columns Go to KM Value Search

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KM VALUE [mM]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.03

1-O-indol-3-yl-acetyl-beta-D-glucose

0.83 - 4.1

myo-inositol

4 entries

0.83

myo-inositol

recombinant enzyme from Saccharomyces cerevisiae, at pH 7.4 and 30°C

myo-inositol

recombinant enzyme from Escherichia coli, at pH 7.4 and 30°C

1.38

myo-inositol

native enzyme, at pH 7.4 and 30°C

4.1

myo-inositol

show all columns Go to IC50 Value Search

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IC50 VALUE [mM]

INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

2.2 - 6.7

phenylmethylsulfonyl fluoride

6 entries

2.2

phenylmethylsulfonyl fluoride

Oryza sativa Japonica Group

recombinant enzyme from Escherichia coli, in the presence of 4.4 mM myo-inositol, at pH 7.4 and 30°C

2.5

phenylmethylsulfonyl fluoride

Oryza sativa Japonica Group

recombinant enzyme from Saccharomyces cerevisiae, in the presence of 4.4 mM myo-inositol, at pH 7.4 and 30°C

3.7

phenylmethylsulfonyl fluoride

Oryza sativa Japonica Group

native enzyme, in the presence of 4.4 mM myo-inositol, at pH 7.4 and 30°C

phenylmethylsulfonyl fluoride

Oryza sativa Japonica Group

recombinant enzyme from Saccharomyces cerevisiae, in the presence of 8.1 mM myo-inositol, at pH 7.4 and 30°C

phenylmethylsulfonyl fluoride

Oryza sativa Japonica Group

recombinant enzyme from Escherichia coli, in the presence of 8.1 mM myo-inositol, at pH 7.4 and 30°C

6.7

phenylmethylsulfonyl fluoride

Oryza sativa Japonica Group

native enzyme, in the presence of 8.1 mM myo-inositol, at pH 7.4 and 30°C

show all columns Go to Specific Activity Search

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SPECIFIC ACTIVITY [µmol/min/mg]

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

0.00501

native enzyme, at pH 7.4 and 30°C

0.01809

recombinant enzyme from Escherichia coli, at pH 7.4 and 30°C

0.01875

show all columns Go to pH Optimum Search

recombinant enzyme from Saccharomyces cerevisiae, at pH 7.4 and 30°C

13.3

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pH OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

6.9

487444

7.4

additional information

pI: 6.1

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TEMPERATURE OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

assay at

assay at

show all columns Go to Pi Value Search

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pI VALUE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

5.5

recombinant enzyme from Escherichia coli, calculated from amino acid sequence

5.5

native enzyme, calculated from amino acid sequence

5.5

recombinant enzyme from Saccharomyces cerevisiae, calculated from amino acid sequence

show all columns Go to Organism Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks include all textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks + FRENDAco-occurrence of enzyme names and organism names (less precise)

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ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

UniProt

brenda

487444, 487445, 660072

brenda

sweet corn, var. Seneca Horizon

brenda

show all columns Go to Source Tissue Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

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SOURCE TISSUE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

SOURCE

immature

brenda

brenda

brenda

endosperm

brenda

Highest Expressing Human Cell Lines

Filter by:

Cell Line Links

Gene Links

Go to AA Sequence and Transmembrane Helices SearchGo to Localization Prediction

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UNIPROT

ENTRY NAME

ORGANISM

NO. OF AA

NO. OF TRANSM. HELICES

MOLECULAR WEIGHT[Da]

SOURCE

SEQUENCE

LOCALIZATION PREDICTION

The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).

B9EZV5 pBLAST

B9EZV5_ORYSJ

Oryza sativa subsp. japonica

481

54220

TrEMBL

Show Sequence

Secretory Pathway (Reliability: 2)

show all columns Go to Molecular Weight Search

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MOLECULAR WEIGHT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

100000

MW below 100000, gel filtration

59000

gel filtration

654000

1 * 654000, enzyme exists as both a monomeric and homo- or heterodimeric form, SDS-PAGE

show all columns Go to Subunit Search

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SUBUNIT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

5 entries

dimer

enzyme exists as both a monomeric and homo- or heterodimeric form

monomer

1 * 654000, enzyme exists as both a monomeric and homo- or heterodimeric form, SDS-PAGE

x * 54300, native enzyme, calculated from amino acid sequence

x * 54500, recombinant enzyme from Saccharomyces cerevisiae, calculated from amino acid sequence

x * 58000, recombinant enzyme from Escherichia coli, calculated from amino acid sequence

x * 71000, native enzyme or recombinant enzyme from Saccharomyces cerevisiae, SDS-PAGE

x * 58000, recombinant enzyme from Escherichia coli, SDS-PAGE

show all columns Go to Posttranslational Modification Search

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POSTTRANSLATIONAL MODIFICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

glycoprotein

glycoprotein

glycosylation is not necessary for enzyme activity

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

Go to General Stability Search

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GENERAL STABILITY

ORGANISM

UNIPROT

LITERATURE

lyophilization, stable to

Go to Storage Stability Search

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STORAGE STABILITY

ORGANISM

UNIPROT

LITERATURE

-20°C, crude liquid endosperm, several years, no loss of activity

4°C, more than 2 months

Go to Purification (commentary) Search

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PURIFICATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

487446, 660072

ConA-agarose column chromatography

Go to Cloned (commentary) Search

partial

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CLONED (Commentary)

ORGANISM

UNIPROT

LITERATURE

expressed in Saccharomyces cerevisiae strain InvSc1 and Escherichia coli strain BL21-CodonPlus(DE3)-RIL

Go to Renatured Search

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RENATURED/Commentary

ORGANISM

UNIPROT

LITERATURE

recombinant enzyme from Escherichia coli, using 50 mM Tris-HCl buffer pH 8.5 containing 9.6 mM NaCl, 0.4 mM KCl, 2 mM MgCl2, 2 mM CaCl2, 0.5M arginin, 0.4 M sucrose, 0.75 mM guanidine hydrochloride, 1 mM GSH and 0.1 mM GSSH

top print hide References Search

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REF.

AUTHORS

TITLE

JOURNAL

VOL.

PAGES

YEAR

ORGANISM (UNIPROT)

PUBMED ID

SOURCE

487444

Michalczuk, L.; Bandurski, R.S.

Enzymic synthesis of 1-O-indol-3-ylacetyl-beta-D-glucose and indol-3-ylacetyl-myo-inositol

Biochem. J.

207

273-281

1982

Zea mays

6218801

brenda

487445

Michalczuk, L.; Bandurski, R.S.

UDP-glucose: indoleacetic acid glucosyl transferase and indoleacetyl-glucose: myo-inositol indoleacetyl transferase

Biochem. Biophys. Res. Commun.

588-592

1980

Zea mays

6446303

brenda

Kesy, J.M.; Bandurski, R.S.

Partial purification and characterization of indol-3-ylacetylglucoe:myo-inositol indol-3-ylacetyltransferase (indoleacetic acid-inositol synthase)

Plant Physiol.

1598-1604

1990

Zea mays

11537469

brenda

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

Physiol. Plant.

119

165-174

2003

Zea mays

brenda