Literature summary for 4.3.3.7 extracted from

Sowole, M.A.; Simpson, S.; Skovpen, Y.V.; Palmer, D.R.; Konermann, L.
Evidence of allosteric enzyme regulation via changes in conformational dynamics A hydrogen/deuterium exchange investigation of dihydrodipicolinate synthase (2016), Biochemistry, 55, 5413-5422 .

Search for more literature for 4.3.3.7

Application

Application	Comment	Organism
drug development	the enzyme is a promising antibiotic target	Campylobacter jejuni
pharmacology	the enzyme is a promising antibiotic target	Campylobacter jejuni

Inhibitors

Inhibitors	Comment	Organism	Structure
bis-lysine	-	Campylobacter jejuni
L-lysine	allosteric inhihitor. Allostery is mediated by changes in the extent of thermally activated conformational fluctuations	Campylobacter jejuni

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
pyruvate + L-aspartate-4-semialdehyde	Campylobacter jejuni	-	(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O	-	?

Organism

Organism	UniProt	Comment	Textmining
Campylobacter jejuni	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
pyruvate + L-aspartate-4-semialdehyde	-	Campylobacter jejuni	(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O	-	?

Subunits

Subunits	Comment	Organism
tetramer	-	Campylobacter jejuni

Synonyms

Synonyms	Comment	Organism
CjDHDPS	-	Campylobacter jejuni

General Information

General Information	Comment	Organism
metabolism	the enzyme catalyzes a step of the diaminopimelate biosynthetic pathway of lysine	Campylobacter jejuni

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Release 2023.1 (January 2023)