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Literature summary for 2.3.1.47 extracted from

  • Ploux, O.; Breyne, O.; Carillon, S.; Marquet, A.
    Slow-binding and competitive inhibition of 8-amino-7-oxopelargonate synthase, a pyridoxal-5'-phosphate-dependent enzyme involved in biotin biosynthesis, by substrate and intermediate analogs: kinetic and binding studies (1999), Eur. J. Biochem., 259, 63-70.
    View publication on PubMed

Application

Application Comment Organism
agriculture possible target for design of inhibitors as herbicides and antibacterial agents Lysinibacillus sphaericus

Inhibitors

Inhibitors Comment Organism Structure
2-amino-3-hydroxy-2-methylnonadioic acid competitive, transition state analogue Lysinibacillus sphaericus
4-carboxybutyl(1-amino-1-carboxyethyl)phosphonate competitive, transition state analogue Lysinibacillus sphaericus
8-amino-7-oxo-8-phosphonononanoic acid strong inhibition Lysinibacillus sphaericus
D-alanine competitive; Schiff base formation between D- or L-alanine and pyridoxal-5'-phophate in the active site Lysinibacillus sphaericus
additional information inhibition mechanism; no inhibition by 8-amino-7-oxo-8-phosphonononanoic acid Lysinibacillus sphaericus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6-carboxyhexanoyl-CoA + L-alanine Lysinibacillus sphaericus i.e. pimeloyl-CoA 8-amino-7-oxononanoate + CoA + CO2 i.e. 7-oxo-8-amino-pelargonic acid ir
6-carboxyhexanoyl-CoA + L-alanine Lysinibacillus sphaericus second step in biotin biosynthesis 8-amino-7-oxononanoate + CoA + CO2 i.e. 7-oxo-8-amino-pelargonic acid ir
6-carboxyhexanoyl-CoA + L-alanine Lysinibacillus sphaericus reaction in biotin biosynthesis 8-amino-7-oxononanoate + CoA + CO2 i.e. 7-oxo-8-amino-pelargonic acid ir

Organism

Organism UniProt Comment Textmining
Lysinibacillus sphaericus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant from E. coli overproducing strain Lysinibacillus sphaericus

Reaction

Reaction Comment Organism Reaction ID
pimeloyl-[acyl-carrier protein] + L-alanine = 8-amino-7-oxononanoate + CO2 + holo-[acyl-carrier protein] binding study of L-alanine and D-alanine to the enzyme Lysinibacillus sphaericus
pimeloyl-[acyl-carrier protein] + L-alanine = 8-amino-7-oxononanoate + CO2 + holo-[acyl-carrier protein] Schiff base formation between D- or L-alanine and pyridoxal-5'-phophate in the active site Lysinibacillus sphaericus
pimeloyl-[acyl-carrier protein] + L-alanine = 8-amino-7-oxononanoate + CO2 + holo-[acyl-carrier protein] binding of pimeloyl-CoA causes a conformational change in the active site Lysinibacillus sphaericus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6-carboxyhexanoyl-CoA + L-alanine i.e. pimeloyl-CoA Lysinibacillus sphaericus 8-amino-7-oxononanoate + CoA + CO2 i.e. 7-oxo-8-amino-pelargonic acid ir
6-carboxyhexanoyl-CoA + L-alanine second step in biotin biosynthesis Lysinibacillus sphaericus 8-amino-7-oxononanoate + CoA + CO2 i.e. 7-oxo-8-amino-pelargonic acid ir
6-carboxyhexanoyl-CoA + L-alanine reaction in biotin biosynthesis Lysinibacillus sphaericus 8-amino-7-oxononanoate + CoA + CO2 i.e. 7-oxo-8-amino-pelargonic acid ir

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Lysinibacillus sphaericus

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate Schiff base formation between D- or L-alanine and pyridoxal-5'-phophate in the active site Lysinibacillus sphaericus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.007
-
8-amino-7-oxo-8-phosphonononanoic acid
-
Lysinibacillus sphaericus
0.068
-
4-carboxybutyl(1-amino-1-carboxyethyl)phosphonate
-
Lysinibacillus sphaericus
0.08
-
2-amino-3-hydroxy-2-methylnonadioic acid
-
Lysinibacillus sphaericus
0.59
-
D-alanine
-
Lysinibacillus sphaericus