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Literature summary for 2.3.1.4 extracted from

  • Vessal, M.; Jaberi-Pour, M.
    Partial purification and kinetic properties of three different D-glucosamine 6-P:N-acetyltransferase forms from human placenta (1998), Comp. Biochem. Physiol. B, 121B, 379-384.
No PubMed abstract available
Search for more literature for 2.3.1.4

Inhibitors

Inhibitors Comment Organism Structure
p-hydroxymercuribenzoate 2.5 mM, 81% inhibition of isoenzyme 1, 92% inhibition of isoenzyme 2 and 92.5% inhibition of isoenzyme 3, inhibition by 1.25 mM is reversible upon addition of 2.5 mM dithiothreitol Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.157
-
 acetyl-CoA isoenzyme 1 Homo sapiens
0.187
-
 acetyl-CoA isoenzyme 2 Homo sapiens
0.28
-
 acetyl-CoA isoenzyme 3 Homo sapiens
3
-
 D-glucosamine 6-phosphate isoenzymes 2 and 3 Homo sapiens
7.1
-
 D-glucosamine 6-phosphate isoenzyme 1 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
 3 isoenzymes
-

Purification (Commentary)

Purification (Comment) Organism
isoenzymes 1-3, CM-Sephadex Homo sapiens

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.00447
-
 isoenzymes 1 and 2 Homo sapiens
0.0379
-
 isoenzyme 3 Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + D-glucosamine 6-phosphate
-
 Homo sapiens CoA + N-acetyl-D-glucosamine 6-phosphate
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9.7
-
 in glycine-NaOH Homo sapiens