KEGG   ENZYME: 4.1.2.8
Entry
EC 4.1.2.8                  Enzyme                                 
Name
indole-3-glycerol-phosphate lyase;
tryptophan synthase alpha;
TSA;
indoleglycerolphosphate aldolase;
indole glycerol phosphate hydrolase;
indole synthase;
indole-3-glycerolphosphate D-glyceraldehyde-3-phosphate-lyase;
indole-3-glycerol phosphate lyase;
IGL;
BX1;
(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate D-glyceraldehyde-3-phosphate-lyase
Class
Lyases;
Carbon-carbon lyases;
Aldehyde-lyases
Sysname
(1S,2R)-1-C-(indol-3-yl)glycerol-3-phosphate D-glyceraldehyde-3-phosphate-lyase (indole-forming)
Reaction(IUBMB)
(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate = indole + D-glyceraldehyde 3-phosphate [RN:R02340]
Reaction(KEGG)
R02340
Substrate
(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate [CPD:C03506]
Product
indole [CPD:C00463];
D-glyceraldehyde 3-phosphate [CPD:C00118]
Comment
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].
History
EC 4.1.2.8 created 1961, deleted 1972, reinstated 2006
Pathway
ec00402  Benzoxazinoid biosynthesis
ec00999  Biosynthesis of various plant secondary metabolites
ec01100  Metabolic pathways
Orthology
K13222  indole-3-glycerol-phosphate lyase
Genes
AJM119046283
OSA4334427 9268807 9270552
DOSAOs03t0797400-01(Os03g0797400) Os03t0797500-01(Os03g0797500)
OBR102712344 102719945
BDI100834829 100836811 100843076
ATS109757378 109757925 109758460 109758461 109758465 109758467
TDC119266786 119274497 119288742 119293741 119300212 119300215 119300216 119300220 119303553 119306451 119310336 119312209
TAES123057652 123064487 123076902 123100031 123101657 123105414 123105418 123108041 123113684 123113689 123113690 123117220 123121015 123123211 123123214 123125768 543409 606350
TUA125506147 125506148 125506150 125506153 125506154 125506155 125542439 125553965
SBI8061167 8081255
ZMA100273163 103644182 542117
SITA101766758 101767173
SVS117836702 117836952 117840141
PVIR120649457 120649458 120687605 120694218 120694220 120703101 120703103 120703106 120703107 120703108 120703119 120703120
PHAI112875875 112875946 112876216
 » show all
Reference
1  [PMID:13376586]
  Authors
YANOFSKY C.
  Title
The enzymatic conversion of anthranilic acid to indole.
  Journal
J Biol Chem 223:171-84 (1956)
Reference
2  [PMID:9235894]
  Authors
Frey M, Chomet P, Glawischnig E, Stettner C, Grun S, Winklmair A, Eisenreich W, Bacher A, Meeley RB, Briggs SP, Simcox K, Gierl A.
  Title
Analysis of a chemical plant defense mechanism in grasses.
  Journal
Science 277:696-9 (1997)
DOI:10.1126/science.277.5326.696
  Sequence
[zma:542117]
Reference
3  [PMID:11106389]
  Authors
Frey M, Stettner C, Pare PW, Schmelz EA, Tumlinson JH, Gierl A.
  Title
An herbivore elicitor activates the gene for indole emission in maize.
  Journal
Proc Natl Acad Sci U S A 97:14801-6 (2000)
DOI:10.1073/pnas.260499897
Reference
4  [PMID:9371848]
  Authors
Melanson D, Chilton MD, Masters-Moore D, Chilton WS
  Title
A deletion in an indole synthase gene is responsible for the DIMBOA-deficient phenotype of bxbx maize.
  Journal
Proc Natl Acad Sci U S A 94:13345-50 (1997)
DOI:10.1073/pnas.94.24.13345
Other DBs
ExplorEnz - The Enzyme Database: 4.1.2.8
IUBMB Enzyme Nomenclature: 4.1.2.8
ExPASy - ENZYME nomenclature database: 4.1.2.8
BRENDA, the Enzyme Database: 4.1.2.8
CAS: 9014-52-2
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