4.1.2.8: indole-3-glycerol-phosphate lyase

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For detailed information about indole-3-glycerol-phosphate lyase, go to the full flat file.

Reaction

Synonyms

BX1, IGL, indole synthase, indole-3-glycerol phosphate lyase, indole-3-glycerophosphate D-glyceraldehyde-3-phosphate-lyase, indoleglycerolphosphate hydrolase, INS, Os03g58300, OSJNBa0094F01.14, PtIGL, TRPS, tryptophan synthase alpha, tryptophan synthase alpha subunit, TSA, Tsa1, ZmTSA

ECTree

     4 Lyases

         4.1 Carbon-carbon lyases

             4.1.2 Aldehyde-lyases

                4.1.2.8 indole-3-glycerol-phosphate lyase

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1	Activating Compound
7	AA Sequence
1	CAS Registry Number
6	Cloned(Commentary)
3	Crystallization (Commentary)
1	Expression
2	General Information
7	Inhibitors
1	kcat/KM [mM/s]
3	KM Value [mM]
4	Localization
8	Natural Substrates/ Products (Substrates)
15	Organism
6	Pathway
1	pH Optimum
5	Protein Variants
3	Purification (Commentary)
2	Reaction
15	Reference
12	Source Tissue
15	Substrates and Products (Substrate)
1	Subunits
23	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]
3	Turnover Number [1/s]

Crystallization

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

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

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Salmonella enterica subsp. enterica serovar Typhimurium

-

691963

the crystal structure of tryptophan synthase is determined at 2.1 A resolution

Salmonella enterica subsp. enterica serovar Typhimurium

-

691784

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

Zea mays

P42390

666055