BRENDA - Enzyme Database
show all sequences of 4.1.2.8

Transcriptional activation of Igl, the gene for indole formation in Zea mays: a structure-activity study with elicitor-active N-acyl glutamines from insects

Frey, M.; Spiteller, D.; Boland, W.; Gierl, A.; Phytochemistry 65, 1047-1055 (2004)

Data extracted from this reference:

Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
indole-3-glycerol phosphate
Zea mays
the indole-3-glycerol phosphate lyase Igl is the structural gene of volatile indole biosynthesis in the tritrophic interaction in maize. The gene is activated on transcriptional level with the same kinetics and to the same level by the fatty acid amino acid conjugates volicitin and N-linolenoyl-L-glutamine. Both conjugates are present in the regurgitates of herbivorous caterpillars. Modifications of the fatty acid moiety of the fatty acid amino acid conjugates greatly reduces the elicitation of Igl and only the L-stereoisomer of the fatty acid amino acid conjugates shows biological activity in the system. Volicitin treatment leads to a fast increase of allene oxide synthase and allene oxide cyclase transcription levels and methyl jasmonate application induces Igl transcription. Hence,the induction of jasmonate biosynthesis appears to be an integral part of the elicitor mediated increase of Igl gene transcription
indole + glyceraldehyde 3-phosphate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Zea mays
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
indole-3-glycerol phosphate
-
670511
Zea mays
indole + glyceraldehyde 3-phosphate
-
-
-
?
indole-3-glycerol phosphate
the indole-3-glycerol phosphate lyase Igl is the structural gene of volatile indole biosynthesis in the tritrophic interaction in maize. The gene is activated on transcriptional level with the same kinetics and to the same level by the fatty acid amino acid conjugates volicitin and N-linolenoyl-L-glutamine. Both conjugates are present in the regurgitates of herbivorous caterpillars. Modifications of the fatty acid moiety of the fatty acid amino acid conjugates greatly reduces the elicitation of Igl and only the L-stereoisomer of the fatty acid amino acid conjugates shows biological activity in the system. Volicitin treatment leads to a fast increase of allene oxide synthase and allene oxide cyclase transcription levels and methyl jasmonate application induces Igl transcription. Hence,the induction of jasmonate biosynthesis appears to be an integral part of the elicitor mediated increase of Igl gene transcription
670511
Zea mays
indole + glyceraldehyde 3-phosphate
-
-
-
?
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
indole-3-glycerol phosphate
Zea mays
the indole-3-glycerol phosphate lyase Igl is the structural gene of volatile indole biosynthesis in the tritrophic interaction in maize. The gene is activated on transcriptional level with the same kinetics and to the same level by the fatty acid amino acid conjugates volicitin and N-linolenoyl-L-glutamine. Both conjugates are present in the regurgitates of herbivorous caterpillars. Modifications of the fatty acid moiety of the fatty acid amino acid conjugates greatly reduces the elicitation of Igl and only the L-stereoisomer of the fatty acid amino acid conjugates shows biological activity in the system. Volicitin treatment leads to a fast increase of allene oxide synthase and allene oxide cyclase transcription levels and methyl jasmonate application induces Igl transcription. Hence,the induction of jasmonate biosynthesis appears to be an integral part of the elicitor mediated increase of Igl gene transcription
indole + glyceraldehyde 3-phosphate
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
indole-3-glycerol phosphate
-
670511
Zea mays
indole + glyceraldehyde 3-phosphate
-
-
-
?
indole-3-glycerol phosphate
the indole-3-glycerol phosphate lyase Igl is the structural gene of volatile indole biosynthesis in the tritrophic interaction in maize. The gene is activated on transcriptional level with the same kinetics and to the same level by the fatty acid amino acid conjugates volicitin and N-linolenoyl-L-glutamine. Both conjugates are present in the regurgitates of herbivorous caterpillars. Modifications of the fatty acid moiety of the fatty acid amino acid conjugates greatly reduces the elicitation of Igl and only the L-stereoisomer of the fatty acid amino acid conjugates shows biological activity in the system. Volicitin treatment leads to a fast increase of allene oxide synthase and allene oxide cyclase transcription levels and methyl jasmonate application induces Igl transcription. Hence,the induction of jasmonate biosynthesis appears to be an integral part of the elicitor mediated increase of Igl gene transcription
670511
Zea mays
indole + glyceraldehyde 3-phosphate
-
-
-
?
Other publictions for EC 4.1.2.8
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
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Salmonella enterica subsp. enterica serovar Typhimurium
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Transcriptional activation of ...
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Phytochemistry
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2004
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