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Literature summary extracted from

  • Dopkins, B.; Tipton, P.; Thoden, J.; Holden, H.
    Structural studies on a glucosamine/glucosaminide N-acetyltransferase (2016), Biochemistry, 55, 4495-4508 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.3 structures of crystals obtained at pH 5 and pH 8 and in complex with either substrate or product Clostridium acetobutylicum

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.3 D287N residue is important for substrate binding but has no critical roles as acid/base catalysts Clostridium acetobutylicum
2.3.1.3 Y297F residue is important for substrate binding but has no critical roles as acid/base catalysts Clostridium acetobutylicum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.3 0.012
-
 acetyl-CoA pH 7.3, 25°C Clostridium acetobutylicum
2.3.1.3 0.21
-
 D-glucosamine pH 7.3, 25°C Clostridium acetobutylicum

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.3 Clostridium acetobutylicum
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.3 acetyl-CoA + D-glucosamine
-
 Clostridium acetobutylicum CoA + N-acetyl-D-glucosamine
-
 ?
2.3.1.3 additional information GlmA follows an ordered mechanism with acetyl CoA binding first followed by glucosamine. The product N-acetylglucosamine is then released prior to CoA Clostridium acetobutylicum ?
-
-

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.3.1.3 2.5
-
 acetyl-CoA pH 7.3, 25°C Clostridium acetobutylicum

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.3.1.3 12
-
 D-glucosamine pH 7.3, 25°C Clostridium acetobutylicum
2.3.1.3 210
-
 acetyl-CoA pH 7.3, 25°C Clostridium acetobutylicum