Literature summary for 4.2.3.4 extracted from

Nichols, C.E.; Ren, J.; Leslie, K.; Dhaliwal, B.; Lockyer, M.; Charles, I.; Hawkins, A.R.; Stammers, D.K.
Comparison of ligand-induced conformational changes and domain closure mechanisms, between prokaryotic and eukaryotic dehydroquinate synthases (2004), J. Mol. Biol., 343, 533-546.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
sitting-drop vapour-diffusion crystallisation at 4°C utilising microbridges, crystals of unliganded enzyme as well as in complexes with NAD+, the substrate analogue [1R-(1alpha,3beta,4alpha,5beta)]-5-phosphonomethyl-1,3,4-trihydroxycyclohexane-1-carboxylic acid and together with both, NAD+ and [1R-(1alpha,3beta,4alpha,5beta)]-5-phosphonomethyl-1,3,4-trihydroxycyclohexane-1-carboxylic acid	Aspergillus nidulans
sitting-drop vapour-diffusion crystallisation at 4°C utilising microbridges, crystals of unliganded enzyme as well as in complexes with NAD, the substrate analogue [1R-(1alpha,3beta,4alpha,5beta)]-5-phosphonomethyl-1,3,4-trihydroxycyclohexane-1-carboxylic acid and together with both, NAD and [1R-(1alpha,3beta,4alpha,5beta)]-5-phosphonomethyl-1,3,4-trihydroxycyclohexane-1-carboxylic acid	Staphylococcus aureus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Co2+	-	Aspergillus nidulans
Co2+	-	Staphylococcus aureus

Organism

Organism	UniProt	Comment	Textmining
Aspergillus nidulans	P07547	-	-
Staphylococcus aureus	Q6GGU4	-	-

Synonyms

Synonyms	Comment	Organism
dehydroquinate synthase	-	Aspergillus nidulans
dehydroquinate synthase	-	Staphylococcus aureus

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Aspergillus nidulans
NAD+	-	Staphylococcus aureus

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Release 2023.1 (January 2023)