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Literature summary extracted from

  • Ehmann, D.E.; Gehring, A.M.; Walsh, C.T.
    Lysine biosynthesis in Saccharomyces cerevisiae: mechanism of alpha-aminoadipate reductase (Lys2) involves posttranslational phosphopantetheinylation by Lys5 (1999), Biochemistry, 38, 6171-6177.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.1.31 Lys5 and Lys2 cloned from Saccharomyces cerevisiae DNA, overexpressed in Escherichia coli, and purified, Lys5/Lys2 pair is a two component system in which Lys5 covalently primes Lys2, allowing alpha-aminoadipate reductase activity by holo-Lys2 with catalytic cycles of autoaminoacylation and reductive clevage Saccharomyces cerevisiae
1.2.1.95 expression in ERscherichia coli Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.31 0.62
-
 NADPH of Lys2 Saccharomyces cerevisiae
1.2.1.95 0.43
-
 S-carboxymethyl-L-cysteine pH 8.8, 37°C Saccharomyces cerevisiae
1.2.1.95 0.47
-
 L-2-aminoadipate pH 8.8, 37°C Saccharomyces cerevisiae
1.2.1.95 0.62
-
 NADPH pH 8.8, 37°C Saccharomyces cerevisiae
1.2.1.95 2.7
-
 D-2-aminoadipate pH 8.8, 37°C Saccharomyces cerevisiae
1.2.1.95 10
-
 adipate pH 8.8, 37°C Saccharomyces cerevisiae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.1.31 31000
-
 Lys5 from induced E. coli cells Saccharomyces cerevisiae
1.2.1.31 155000
-
 full-length Lys2 from induced E. coli cells Saccharomyces cerevisiae
1.2.1.95 155000
-
 x * 155000, calculated Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.31 L-alpha-aminoadipate + NAD(P)H Saccharomyces cerevisiae
-
 L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.31 Saccharomyces cerevisiae
-
-
-
1.2.1.95 Saccharomyces cerevisiae P07702
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.2.1.31 additional information Lys5 demonstrates phosphopantetheinyl transferase activity toward the 14-kDa Lys2 peptidyl carrier protein fragment, with a Km of 0.001 mM and a turnover number of 3/min Saccharomyces cerevisiae
1.2.1.31 side-chain modification Lys5 is a specific posttranslational modification catalyst, using coenzyme A as a cosubstrate to phosphopantetheinylate Ser880 of the Lys2 activating it for catalysis Saccharomyces cerevisiae
1.2.1.95 side-chain modification residue Ser880 is modified by phosphopantetheinylate, leading to activiation of the enzyme. Protein Lys5 catalyzes the modification using coenzyme A Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.31 alpha-aminoadipic semialdehyde + NAD+ + H2O
-
 Saccharomyces cerevisiae alpha-aminoadipic acid + NADH + H+
-
 ?
1.2.1.31 L-2-aminoadipate + NADPH
-
 Saccharomyces cerevisiae L-2-aminoadipate 6-semialdehyde + NADP+ + H2O
-
 ?
1.2.1.31 L-alpha-aminoadipate + NAD(P)H
-
 Saccharomyces cerevisiae L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O
-
 ?
1.2.1.95 adipate + NADPH + H+ + ATP
-
 Saccharomyces cerevisiae adipate semialdehyde + NADP+ + AMP + diphosphate
-
 ?
1.2.1.95 D-2-aminoadipate + NADPH + H+ + ATP
-
 Saccharomyces cerevisiae (R)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate
-
 ?
1.2.1.95 L-2-aminoadipate + NADPH + H+ + ATP
-
 Saccharomyces cerevisiae (S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate
-
 ?
1.2.1.95 S-carboxymethyl-L-cysteine + NADPH + H+ + ATP
-
 Saccharomyces cerevisiae S-formylmethyl-L-cysteine + NADP+ + AMP + diphosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
1.2.1.95 ? x * 155000, calculated Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
1.2.1.95 LYS2
-
 Saccharomyces cerevisiae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.2.1.31 11.2
-
 alpha-aminoadipate semialdehyde production from holo-lys2 Saccharomyces cerevisiae
1.2.1.95 0.0045
-
 adipate pH 8.8, 37°C Saccharomyces cerevisiae
1.2.1.95 0.63
-
 D-2-aminoadipate pH 8.8, 37°C Saccharomyces cerevisiae
1.2.1.95 6
-
 S-carboxymethyl-L-cysteine pH 8.8, 37°C Saccharomyces cerevisiae
1.2.1.95 41.7
-
 L-2-aminoadipate pH 8.8, 37°C Saccharomyces cerevisiae

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.2.1.95 0.0005
-
 adipate pH 8.8, 37°C Saccharomyces cerevisiae
1.2.1.95 0.23
-
 D-2-aminoadipate pH 8.8, 37°C Saccharomyces cerevisiae
1.2.1.95 14
-
 S-carboxymethyl-L-cysteine pH 8.8, 37°C Saccharomyces cerevisiae
1.2.1.95 88.3
-
 L-2-aminoadipate pH 8.8, 37°C Saccharomyces cerevisiae