Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.3.1.3 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
Search for more literature for 2.3.1.3

Crystallization (Commentary)

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

Protein Variants

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Clostridium acetobutylicum
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + D-glucosamine
-
 Clostridium acetobutylicum CoA + N-acetyl-D-glucosamine
-
 ?
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]

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

kcat/KM [mM/s]

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