Literature summary for 5.3.1.24 extracted from

Walker, M.S.; DeMoss, J.A.
Organisation of the functional domains of anthranilate synthase from Neurospora crassa (1986), J. Biol. Chem., 261, 16073-16077.

Search for more literature for 5.3.1.24

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
56000	-	indole-3-glycerol-phosphate synthetase/PRA isomerase fragment of the multifunctional anthranilate synthetase complex beta subunit, gel filtration	Neurospora crassa

Organism

Organism	UniProt	Comment	Textmining
Neurospora crassa	-	a fragment of the beta subunit of the multifunctional alpha2beta2 anthranilate synthetase complex has PRA isomerase and indole-3-glycerol phosphate synthetase activities, organization of the functional domains of the compex	-

Purification (Commentary)

Purification (Comment)	Organism
indole-3-glycerol-phosphate synthetase/PRA isomerase fragment of the multifunctional anthranilate synthetase complex beta subunit	Neurospora crassa

Source Tissue

Source Tissue	Comment	Organism	Textmining
mycelium	-	Neurospora crassa	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
N-(5-phospho-beta-D-ribosyl)anthranilate	-	Neurospora crassa	1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate	-	?

Subunits

Subunits	Comment	Organism
dimer	the indole-3-glycerol-phosphate synthetase/PRA isomerase fragment of the multifunctional anthranilate synthetase complex beta subunit exists as a dimer	Neurospora crassa

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)