Literature summary for 5.3.1.24 extracted from

Hennig, M.; Sterner, R.; Kirschner, K.; Jansonius, J.N.
Crystal structure at 2.0 A resolution of phosphoribosyl anthranilate isomerase from the hyperthermophile Thermotoga maritima: possible determinants of protein stability (1997), Biochemistry, 36, 6009-6016.

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Cloned(Commentary)

Cloned (Comment)	Organism
trpF gene is cloned and expressed in Escherichia coli	Thermotoga maritima

Crystallization (Commentary)

Crystallization (Comment)	Organism
x-ray structure	Thermotoga maritima

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.00028	-	N-(5-phospho-beta-D-ribosyl)anthranilate	pH 7.5, 25°C, dimer	Thermotoga maritima

Organism

Organism	UniProt	Comment	Textmining
Thermotoga maritima	Q56320	monofunctional enzyme	-
Thermotoga maritima	Q56320	Protein Data Bank: 1NSJ	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
N-(5-phospho-beta-D-ribosyl)anthranilate	enzyme structure	Thermotoga maritima	1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate	-	?
N-(5-phospho-beta-D-ribosyl)anthranilate	high catalytic efficiency	Thermotoga maritima	1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate	-	?

Subunits

Subunits	Comment	Organism
homodimer	2 identical (betaalpha)8-barrel subunits, which are associated back-to-back and locked together by a hydrophobic loop	Thermotoga maritima

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
additional information	-	structural features resonsible for the high thermostability	Thermotoga maritima

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Release 2023.1 (January 2023)