4.1.1.48: indole-3-glycerol-phosphate synthase

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

Reaction

Synonyms

eIGPS, IGP synthase, IGPS, indole-3-glycerol phosphate synthase, Indole-3-glycerol phosphate synthetase, Indole-3-glycerol-phosphate synthase, indole-3-glycerolphosphate synthase, Indole-3-glycerophosphate synthase, Indoleglycerol phosphate synthase, Indoleglycerol phosphate synthetase, Indoleglycerolphosphate synthetase, InGP synthase, InGP synthetase, InGPS, mIGPS, MtIGPS, Phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase, Pk-trpC, PRAI, PRAI-InGPS, sIGPS, SSO0895, Synthase, indole-3-glycerol phosphate, TrpC

ECTree

     4 Lyases

         4.1 Carbon-carbon lyases

             4.1.1 Carboxy-lyases

                4.1.1.48 indole-3-glycerol-phosphate synthase

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Results	in table
41425	AA Sequence
5	Application
1	CAS Registry Number
12	Cloned(Commentary)
10	Crystallization (Commentary)
3	Expression
5	General Information
6	General Stability
15	Inhibitors
43	kcat/KM [mM/s]
1	Ki Value [mM]
89	KM Value [mM]
4	Metals/Ions
48	Molecular Weight [Da]
38	Natural Substrates/ Products (Substrates)
1	Organic Solvent Stability
301	Organism
6	Pathway
46	PDB ID
7	pH Optimum
3	pH Range
3	pH Stability
1	Posttranslational Modification
69	Protein Variants
20	Purification (Commentary)
4	Reaction
1	Reaction Type
82	Reference
1	Renatured (Commentary)
2	Source Tissue
9	Specific Activity [micromol/min/mg]
3	Storage Stability
109	Substrates and Products (Substrate)
22	Subunits
77	Synonyms
1	Systematic Name
8	Temperature Optimum [°C]
2	Temperature Range [°C]
20	Temperature Stability [°C]
59	Turnover Number [1/s]

Organic Solvent Stability

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Organic Solvent Stability on EC 4.1.1.48 - indole-3-glycerol-phosphate synthase

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ORGANIC SOLVENT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

urea

Saccharolobus solfataricus

Q06121

the structure of partially folded states of the enzyme is assessed by hydrogen exchange mass spectrometry and Gö model simulations. HX-MS analysis of the peptic peptides derived from the pulse-labeled product of the submillisecond folding reaction from the urea-denatured state reveal strong protection in the (betaalpha)4 region, modest protection in the neighboring (betaalpha)1–3 and (betaalpha)5beta6 segments and no significant protection in the remaining N and C-terminal segments. The results demonstrate that this species is not a collapsed form of the unfolded state under native-favoring conditions nor is it the native state formed via fast-track folding

681463