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Literature summary for 1.4.1.15 extracted from

  • Neshich, I.A.; Kiyota, E.; Arruda, P.
    Genome-wide analysis of lysine catabolism in bacteria reveals new connections with osmotic stress resistance (2013), ISME J., 7, 240-2410.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.4.1.15

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-lysine + NAD+ Ruegeria pomeroyi
-
 1,2-didehydropiperidine-2-carboxylate + NH3 + NADH + H+
-
 r

Organism

Organism UniProt Comment Textmining
Ruegeria pomeroyi
-
 gene lysdh
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-lysine + NAD+
-
 Ruegeria pomeroyi 1,2-didehydropiperidine-2-carboxylate + NH3 + NADH + H+
-
 r
additional information LysDH directly converts L-lysine to alpha-aminoadipic-delta-semialdehyde Ruegeria pomeroyi ?
-
 ?

Synonyms

Synonyms Comment Organism
LysDH
-
 Ruegeria pomeroyi

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Ruegeria pomeroyi
NADH
-
 Ruegeria pomeroyi

Expression

Organism Comment Expression
Ruegeria pomeroyi gene lysdh is not upregulated under salt stress, in contrast to several other enzymes from the lysine-to-alpha-aminoadipic-delta-semialdehyde pathways, but is upregulated by addition of exogenous lysine additional information

General Information

General Information Comment Organism
evolution genomic organization and functional role of lysine catabolic pathways among prokaryotes, overview Ruegeria pomeroyi
physiological function the enzyme is part of the lysine-to alpha-aminoadipic-delta-semialdehyde-pathway, that has a broad evolutionary importance in osmotic stress resistance Ruegeria pomeroyi