KEGG   ENZYME: 4.1.2.8Help
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
BRITE hierarchy
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)
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
Benzoxazinoid biosynthesis
Biosynthesis of secondary metabolites
Orthology
K13222  
indole-3-glycerol-phosphate lyase
Genes
OSA: 
DOSA: 
Os03t0797400-01(Os03g0797400)
BDI: 
SBI: 
SORBI_01g005140(SORBIDRAFT_01g005140) SORBI_01g005150(SORBIDRAFT_01g005150)
ZMA: 
100273163(csu868(trp)) 542117(bx1)
SITA: 
Taxonomy
Reference
1  [PMID:13376586]
  Authors
YANOFSKY C.
  Title
The enzymatic conversion of anthranilic acid to indole.
  Journal
J. Biol. Chem. 223 (1956) 171-84.
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 (1997) 696-9.
  Organism
Zea mays [GN:zma]
  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 (2000) 14801-6.
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 (1997) 13345-50.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9014-52-2

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