Literature summary for 1.2.1.31 extracted from

Guo, S.; Evans, S.A.; Wilkes, M.B.; Bhattacharjee, J.K.
Novel posttranslational activation of the LYS2-encoded.alpha-aminoadipate reductase for biosynthesis of lysine and site-directed mutational analysis of conserved amino acid residues in the activation domain of Candida albicans (2001), J. Bacteriol., 183, 7120-7125.

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Cloned(Commentary)

Cloned (Comment)	Organism
heterlogous expressed in Escherichia coli	Candida albicans

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
L-alpha-aminoadipate + NAD(P)H	Candida albicans	-	L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O	-	?

Organism

Organism	UniProt	Comment	Textmining
Candida albicans	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
additional information	specific amino acid residues, namely G882 and S884 of the Lys2p activation domain are required, the phosphopantetheinyl transferase is required for the activation of Lys2p and not for its alpha-aminoadipate reductase activity	Candida albicans
side-chain modification	the 150-kDa Lys2p is posttranslational modified in the presence of coenzyme A and Candida albicans lys2 mutant extract as a source of phosphopantetheinyl transferase	Candida albicans

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
additional information	-	-	Candida albicans

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-alpha-aminoadipate + NAD(P)H	-	Candida albicans	L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O	-	?

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Release 2023.1 (January 2023)