Information on EC 4.1.2.8 - indole-3-glycerol-phosphate lyase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
4.1.2.8
reinstated 2006, had been eliminated in 1972
RECOMMENDED NAME
GeneOntology No.
indole-3-glycerol-phosphate lyase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate = indole + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate = indole + D-glyceraldehyde 3-phosphate
show the reaction diagram
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
BRENDA Link
KEGG Link
MetaCyc Link
Benzoxazinoid biosynthesis
-
-
DIBOA-glucoside biosynthesis
-
-
L-tryptophan biosynthesis
-
-
NIL
-
-
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].
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
BX1
-
-
BX1
P42390
a homolog of the alpha-subunit of bifunctional trypthophan synthase
IGL
-
-
IGL
Q9FQ77
-
indole synthase
O22765
-
indole synthase
-
-
indole-3-glycerol phosphate lyase
-
-
indole-3-glycerophosphate D-glyceraldehyde-3-phosphate-lyase
-
-
indoleglycerolphosphate hydrolase
-
-
Os03g58300
Q7Y1I9
locus name
OSJNBa0094F01.14
Q7Y1I9
-
tryptophan synthase alpha
O22765
-
tryptophan synthase alpha
-
-
tryptophan synthase alpha subunit
B2Y0K4
-
TSA
-
-
ZmTSA
B2Y0K4
-
CAS REGISTRY NUMBER
COMMENTARY
9014-52-2
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subsp. japonica
UniProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
cv. Delprim
-
-
Manually annotated by BRENDA team
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate
indole + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
?
(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate
indole + D-glyceraldehyde 3-phosphate
show the reaction diagram
B2Y0K4
-
-
-
?
(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate
indole + D-glyceraldehyde 3-phosphate
show the reaction diagram
O22765
-
-
-
?
(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate
indole + D-glyceraldehyde 3-phosphate
show the reaction diagram
Q7Y1I9
-
-
-
?
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
?
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
alpha-site cleaves the C3-C30 bond of IGP
-
-
?
indole-3-glycerol phosphate
indole + glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
?
indole-3-glycerol phosphate
indole + glyceraldehyde 3-phosphate
show the reaction diagram
Q9FQ77
-
-
-
?
indole-3-glycerol phosphate
indole + glyceraldehyde 3-phosphate
show the reaction diagram
P42390
-
-
-
?
indole-3-glycerol phosphate
indole + glyceraldehyde 3-phosphate
show the reaction diagram
-
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
show the reaction diagram
Q9FQ77
Igl transcript level is elevated by volicitin
-
-
?
indole-3-glycerol phosphate
indole + glyceraldehyde 3-phosphate
show the reaction diagram
-
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-3-glycerol phosphate
indole + glyceraldehyde 3-phosphate
show the reaction diagram
P42390
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
-
-
?
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate
indole + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
?
(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate
indole + D-glyceraldehyde 3-phosphate
show the reaction diagram
B2Y0K4
-
-
-
?
(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate
indole + D-glyceraldehyde 3-phosphate
show the reaction diagram
O22765
-
-
-
?
indole-3-glycerol phosphate
indole + glyceraldehyde 3-phosphate
show the reaction diagram
-
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
show the reaction diagram
Q9FQ77
Igl transcript level is elevated by volicitin
-
-
?
indole-3-glycerol phosphate
indole + glyceraldehyde 3-phosphate
show the reaction diagram
-
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-3-glycerol phosphate
indole + glyceraldehyde 3-phosphate
show the reaction diagram
P42390
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
-
-
?
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
-
-
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,3-dihydroxy-3-[(2-hydroxyphenyl)amino] propyl phosphate
-
competetive inhibitor
2-([[4-(trifluoromethoxy)phenyl]sulfonyl]amino) ethyl phosphate
-
competetive inhibitor
3-(1H-indol-3-yl)propyl phosphate
-
competetive inhibitor
3-(2,3-dihydro-1H-indol-3-yl)glycerol phosphate
-
competetive inhibitor
3-acetyl-L-aspartic acid
-
inhibits the alpha-reaction. Indole 3-acetylglycine and 3-acetyl-L-aspartic acid are similar to complexes that are similar to 3-(1H-indol-3-yl)propyl phosphate with the phosphoryl sub-site occupied by the ligand carboxylate, the indole ring NH H-bonded to alphaAsp60, and one carboxylate oxygen of the catalytic alphaGlu49 H-bonded to the acetyl oxygen
-
4-[(2-aminophenyl)sulfonyl]butyl phosphate
-
competetive inhibitor
indole 3-acetylglycine
-
inhibits the alpha-reaction. Indole 3-acetylglycine and 3-acetyl-L-aspartic acid are similar to complexes that are similar to 3-(1H-indol-3-yl)propyl phosphate with the phosphoryl sub-site occupied by the ligand carboxylate, the indole ring NH H-bonded to alphaAsp60, and one carboxylate oxygen of the catalytic alphaGlu49 H-bonded to the acetyl oxygen
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
volicitin
Q9FQ77
activates
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.096
(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate
Q7Y1I9
pH 8.0, 22°C
0.458
(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate
B2Y0K4
-
0.1
indole-3-glycerol phosphate
Q9FQ77
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.006
(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate
B2Y0K4
-
6.55
(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate
Q7Y1I9
pH 8.0, 22°C
2.3
indole-3-glycerol phosphate
Q9FQ77
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
65.15
(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate
Q7Y1I9
pH 8.0, 22°C
17953
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.2
B2Y0K4
tryptophan synthase assay
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
B2Y0K4
tryptophan synthase assay
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
B2Y0K4
-
Manually annotated by BRENDA team
Q9FQ77
Igl is expressed highest in upper parts of the plantlet
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the crystal structure of tryptophan synthase is determined at 2.1 A resolution
-
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
recombinant protein by His-tag affinity purification via Ni-NTA agarose, plant protein by anion exchange and gel permeation chromatography
B2Y0K4
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CaMV35S-INS-GFP and CaMV35-TSA1-GFP are constructed, the INS open reading frame is subcloned into the vector pQE81
O22765
expressed in Escherichia coli
-
expression in Escherichia coli
Q9FQ77
into the vectorS pET28a, pEZS-NL and pPCVE35E
B2Y0K4
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is upregulated by insect feeding
Q7Y1I9
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D60N
-
site-directed mutagenesis, substitution of asparagine for aspartic acid in the alphaAsp60Asn variant. alphaAsp60 has an essential role in stabilizing charge development on the IGP indole ring during C-C bond scission
Q114N
-
betaGln114Asn mutation, which shortens the betaGln114 side chain connecting the betaL3 loop with the rest of the protein, resulted in two fractions of enzyme
T183V
-
site-directed mutagenesis, substitution of valine for threonine in the alphaThr183Val variant, resulting in impaired catalysis at the alpha-site and loss of allosteric communication
Y110V
-
betaThr110Val mutation, which replaces a hydrogen bonding partner to the substrate carboxylate with a methyl group severely decreased the ability to form the aminoacrylate external aldimine E(AA) and consequently severely impaired beta-reaction and alphabeta-reaction