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Literature summary for 1.21.4.1 extracted from

  • Hodgins, D.S.; Abeles, R.H.
    Studies of the mechanism of action of D-proline reductase: the presence on covalently bound pyruvate and its role in the catalytic process (1969), Arch. Biochem. Biophys., 130, 274-285.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
thiol most effective activator towards iodoacetate inhibition Acetoanaerobium sticklandii

Inhibitors

Inhibitors Comment Organism Structure
2-Bromobutyrate
-
Acetoanaerobium sticklandii
2-Bromopropionate
-
Acetoanaerobium sticklandii
3-Bromopropionate
-
Acetoanaerobium sticklandii
Bromoacetate
-
Acetoanaerobium sticklandii
hydroxylamine
-
Acetoanaerobium sticklandii
Hydroxylamine hydrochloride
-
Acetoanaerobium sticklandii
iodoacetamide
-
Acetoanaerobium sticklandii
iodoacetate
-
Acetoanaerobium sticklandii
NaBH4
-
Acetoanaerobium sticklandii
phenylhydrazine
-
Acetoanaerobium sticklandii
phenylhydrazine hydrochloride
-
Acetoanaerobium sticklandii
Sodium borohydride
-
Acetoanaerobium sticklandii

Organism

Organism UniProt Comment Textmining
Acetoanaerobium sticklandii
-
strain ATCC12662 identical with strain DSM 519 T
-

Purification (Commentary)

Purification (Comment) Organism
partially Acetoanaerobium sticklandii

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7
-
-
Acetoanaerobium sticklandii

Storage Stability

Storage Stability Organism
0°C frozen cells maintains essentially full enzyme activity for at least 4 months Acetoanaerobium sticklandii