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Literature summary for 5.4.3.2 extracted from

  • Chirpich, T.P.; Barker, H.A.
    Lysine-2,3-aminomutase (Clostridium) (1971), Methods Enzymol., 17B, 215-222.
No PubMed abstract available
Search for more literature for 5.4.3.2

Activating Compound

Activating Compound Comment Organism Structure
Reducing agent required Clostridium sp.
S-adenosylmethionine activates Clostridium sp.
S-adenosylmethionine Km: 0.00003 mM with 10 mM Lys as substrate Clostridium sp.

Inhibitors

Inhibitors Comment Organism Structure
Co2+ 0.1 mM, 80% inhibition Clostridium sp.
S-adenosylhomocysteine competitive towards S-adenosylmethionine Clostridium sp.
S-aminoethylcysteine
-
 Clostridium sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.6
-
 L-Lys
-
 Clostridium sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
230000
-
 gel filtration Clostridium sp.

Organism

Organism UniProt Comment Textmining
Clostridium sp.
-
-
-
Clostridium sp. SB4
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Clostridium sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.1
-
-
 Clostridium sp.

Storage Stability

Storage Stability Organism
-10°C, 20 mM potassium phosphate buffer, pH 6.7, partially purified enzyme, approximately 25% loss of activity in 2 months Clostridium sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Lys r Clostridium sp. (3S)-3,6-diaminohexanoic acid
-
 ?
L-Lys r Clostridium sp. SB4 (3S)-3,6-diaminohexanoic acid
-
 ?

Cofactor

Cofactor Comment Organism Structure
vitamin B6 enzyme contains 0.9 M per 230000 MW protein Clostridium sp.