Literature summary extracted from

Vogan, E.
Shikimate dehydrogenase structure reveals novel fold (2003), Structure, 11, 902-903.

Natural Substrates/ Products (Substrates)

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
1.1.1.25	additional information	Methanocaldococcus jannaschii	fourth enzyme in the shikimate biosynthetic pathway	?	-	?

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.1.1.25	Methanocaldococcus jannaschii	-	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.1.1.25	additional information	fourth enzyme in the shikimate biosynthetic pathway	Methanocaldococcus jannaschii	?	-	?

Subunits

EC Number	Subunits	Comment	Organism
1.1.1.25	More	the structure reveals an enzyme with a deep cleft, which contains the active site, formed at the junction of two domains. The C-terminal domain is easily recognizable as a Rossmann fold dinucleotide binding domain, responsible for binding the NADP cofactor. The N-terminal substrate binding and dimerization domain, an alpha-beta-alpha sandwich, represents a unique topological fold, structure modeling	Methanocaldococcus jannaschii

Synonyms

EC Number	Synonyms	Comment	Organism
1.1.1.25	SDH	-	Methanocaldococcus jannaschii
1.1.1.25	shikimate 5-dehydrogenase	-	Methanocaldococcus jannaschii

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
1.1.1.25	additional information	dinucleotide cofactor binding domain structure is a Rossmann fold	Methanocaldococcus jannaschii

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)