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Literature summary for 5.1.1.7 extracted from

  • Adams, E.
    Amino acid racemases and epimerases (1972), The Enzymes, 3rd Ed. (Boyer, P. D. , ed. ), 6, 479-507.
No PubMed abstract available
Search for more literature for 5.1.1.7

Activating Compound

Activating Compound Comment Organism Structure
additional information no pyridoxal phosphate requirement Escherichia coli
additional information no pyridoxal phosphate requirement Priestia megaterium

Inhibitors

Inhibitors Comment Organism Structure
hydroxylamine no inhibition Escherichia coli
hydroxylamine no inhibition Priestia megaterium
isoniazid
-
 Escherichia coli
Mercurials
-
 Escherichia coli
additional information
-
 Escherichia coli
additional information no inhibition by deoxypyridioxine Priestia megaterium
Semicarbazide
-
 Escherichia coli
Semicarbazide no inhibition Priestia megaterium

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.7
-
 LL-diaminoheptanedioate at 37°C Priestia megaterium
100
-
 meso-diaminoheptanedioate at 37°C Priestia megaterium

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Priestia megaterium
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Priestia megaterium

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
LL-2,6-Diaminoheptanedioate
-
 Escherichia coli meso-Diaminoheptanedioate
-
 ?
LL-2,6-Diaminoheptanedioate
-
 Priestia megaterium meso-Diaminoheptanedioate
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5 8
-
 Priestia megaterium

pH Range

pH Minimum pH Maximum Comment Organism
6 8.5 pH 6: about 60% of maximal activity, pH 8.5: about 25% of maximal activity Priestia megaterium