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Information on EC 4.1.2.8 - indole-3-glycerol-phosphate lyase and Organism(s) Zea mays and UniProt Accession P42390
for references in articles please use BRENDA:EC4.1.2.8reinstated 2006, had been eliminated in 1972
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4.1.2.8 indole-3-glycerol-phosphate lyaseIUBMB Comments
Forms part of the defence mechanism against insects and microbial pathogens in the grass family, Gramineae, where it catalyses the first committed step in the formation of the cyclic hydroxamic acids 2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one (DIBOA) and 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one (DIMBOA) . This enzyme resembles the alpha-subunit of EC 4.2.1.20, tryptophan synthase , for which, (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate is also a substrate, but, unlike tryptophan synthase, its activity is independent of the beta-subunit and free indole is released .
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Word Map
- 4.1.2.8
- pyridoxal
- l-serine
- l-tryptophan
-
aldimine
- alpha-aminoacrylate
-
alpha-glycerol
-
beta-replacement
- beta-chloro-l-alanine
-
benzoxazinoids
-
yanofsky
- diboa
-
ahmed
The taxonomic range for the selected organisms is: Zea mays
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
tryptophan synthase alpha, tryptophan synthase alpha subunit, indole-3-glycerol phosphate lyase, indole synthase, zmtsa, os03g58300, indole-3-glycerol-phosphate lyase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IGL
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate = indole + D-glyceraldehyde 3-phosphate
the indole is further converted to 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one, a secondary plant metabolite. BX1 cleaves indole-3-glycerol phosphate significantly faster to indole and glyceraldehyde 3-phosphate than the homologous alpha-subunit of tryptophan synthase, EC 4.2.1.20. In the primary metabolism, indole diffuses through the connecting tunnel to the beta-active site where it is condensed with serine to form tryptophan and water
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
(1S,2R)-1-C-(indol-3-yl)glycerol-3-phosphate D-glyceraldehyde-3-phosphate-lyase (indole-forming)
Forms part of the defence mechanism against insects and microbial pathogens in the grass family, Gramineae, where it catalyses the first committed step in the formation of the cyclic hydroxamic acids 2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one (DIBOA) and 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one (DIMBOA) [1]. This enzyme resembles the alpha-subunit of EC 4.2.1.20, tryptophan synthase [3], for which, (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate is also a substrate, but, unlike tryptophan synthase, its activity is independent of the beta-subunit and free indole is released [2].
CAS REGISTRY NUMBER
COMMENTARY
9014-52-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate
indole + D-glyceraldehyde 3-phosphate
-
-
-
?
additional information
?
-
-
indole release activated by beet armyworm and methyl salicylate is preceded by igl gene (encoding indole-3-glycerol phosphate lyase) induction within 1.5 h of treatment and declines within 6 h, induction of the IGL gene expression is not observed with (Z)-3-hexenol treatment
-
-
?
indole-3-glycerol phosphate
indole + glyceraldehyde 3-phosphate
the indole is further converted to 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one, a secondary plant metabolite. BX1 cleaves indole-3-glycerol phosphate significantly faster to indole and glyceraldehyde 3-phosphate than the homologous alpha-subunit of tryptophan synthase, EC 4.2.1.20
-
-
?
indole-3-glycerol phosphate
indole + glyceraldehyde 3-phosphate
-
branch point from tryptophan biosynthesis, the enzyme is required for biosynthesis of 2,4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one
-
-
?
indole-3-glycerol phosphate
indole + glyceraldehyde 3-phosphate
Igl transcript level is elevated by volicitin
-
-
?
indole-3-glycerol phosphate
indole + glyceraldehyde 3-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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
indole-3-glycerol phosphate
indole + glyceraldehyde 3-phosphate
the indole is further converted to 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one, a secondary plant metabolite. BX1 cleaves indole-3-glycerol phosphate significantly faster to indole and glyceraldehyde 3-phosphate than the homologous alpha-subunit of tryptophan synthase, EC 4.2.1.20
-
-
?
(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate
indole + D-glyceraldehyde 3-phosphate
-
-
-
?
additional information
?
-
-
indole release activated by beet armyworm and methyl salicylate is preceded by igl gene (encoding indole-3-glycerol phosphate lyase) induction within 1.5 h of treatment and declines within 6 h, induction of the IGL gene expression is not observed with (Z)-3-hexenol treatment
-
-
?
indole-3-glycerol phosphate
indole + glyceraldehyde 3-phosphate
-
branch point from tryptophan biosynthesis, the enzyme is required for biosynthesis of 2,4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one
-
-
?
indole-3-glycerol phosphate
indole + glyceraldehyde 3-phosphate
Igl transcript level is elevated by volicitin
-
-
?
indole-3-glycerol phosphate
indole + glyceraldehyde 3-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
-
-
?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
in an isoform Igl deficient background, mutant plants deficient in chloroplastic isoform Bx1 allow better development of the cereal aphid Rhopalosiphum padi, and are affected in penetration resistance against the fungus Setosphaeria turtica. At stages preceding major tissue disruption, Rhopalosiphum padi and Setosphaeria turtica elicited increased accumulation of 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one-glucoside, 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one, and 2-hydroxy-4,7-dimethoxy-1,4-benzoxazin-3-one-glucoside (HDMBOA-glc), which is most pronounced in apoplastic leaf extracts. Chloroplastic isoform-deficient bx1 mutant lines deposite less chitosan-induced callose than Bx1 wild-type lines, whereas apoplast infiltration with 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one, but not HDMBOA-glc, mimicks chitosan-induced callose
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).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the crystal structure of BX1 suggusts that the faster catalytic rate of BX1 compared to the homologous alpha-subuni8t of tryptophan synthase EC 4.2.1.20, may due to a stabilzation of the active conformation, loop alphaL6 is closed and the catalytic glutamate, Glu134 is in the active conformation. There are two crystallographically independent molecules in the asymmetric unit of the rhombohedral BX1 crystal form
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kulik, V.; Hartmann, E.; Weyand, M.; Frey, M.; Gierl, A.; Niks, D.; Dunn, M.F.; Schlichting, I.
On the structural basis of the catalytic mechanism and the regulation of the alpha subunit of tryptophan synthase from Salmonella typhimurium and BX1 from maize, two evolutionarily related enzymes
J. Mol. Biol.
352
608-620
2005
Zea mays (P42390)
Frey, M.; Spiteller, D.; Boland, W.; Gierl, A.
Transcriptional activation of Igl, the gene for indole formation in Zea mays: a structure-activity study with elicitor-active N-acyl glutamines from insects
Phytochemistry
65
1047-1055
2004
Zea mays
Farag, M.A.; Fokar, M.; Abd, H.; Zhang, H.; Allen, R.D.; Pare, P.W.
(Z)-3-Hexenol induces defense genes and downstream metabolites in maize
Planta
220
900-909
2005
Zea mays
Melanson, D.; Chilton, M.D.; Masters-Moore, D.; Chilton, W.S.
A deletion in an indole synthase gene is responsible for the DIMBOA-deficient phenotype of bxbx maize
Proc. Natl. Acad. Sci. USA
94
13345-13350
1997
Zea mays (P42390), Zea mays
Frey, M.; Stettner, C.; Pare, P.W.; Schmelz, E.A.; Tumlinson, J.H.; Gierl, A.
An herbivore elicitor activates the gene for indole emission in maize
Proc. Natl. Acad. Sci. USA
97
14801-14806
2000
Zea mays (Q9FQ77), Zea mays
Frey, M.; Chomet, P.; Glawischnig, E.; Stettner, C.; Grun, S.; Winklmair, A.; Eisenreich, W.; Bacher, A.; Meeley, R.B.; Briggs, S.P.; Simcox, K.; Gierl, A.
Analysis of a chemical plant defense mechanism in grasses
Science
277
696-699
1997
Zea mays
Kriechbaumer, V.; Weigang, L.; Fiesselmann, A.; Letzel, T.; Frey, M.; Gierl, A.; Glawischnig, E.
Characterisation of the tryptophan synthase alpha subunit in maize
BMC Plant Biol.
8
44
2008
Zea mays (B2Y0K4), Zea mays
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