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Literature summary extracted from

  • Chou, W.K.; Hinderlich, S.; Reutter, W.; Tanner, M.E.
    Sialic acid biosynthesis: stereochemistry and mechanism of the reaction catalyzed by the mammalian UDP-N-acetylglucosamine 2-epimerase (2003), J. Am. Chem. Soc., 125, 2455-2461.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.183 UDP-GlcNAc 2-epimerase/ManNAc kinase from rat is overexpressed in Spodoptera frugiperda cells (Sf9 cells) using a baculovirus expression system Rattus norvegicus

General Stability

EC Number General Stability Organism
5.1.3.14 the purified enzyme is 80% pure, no further purification because it is unstable to freezing and has limited stability upon storage at 4°C Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.183 0.026
-
 UDP-N-acetyl-alpha-D-glucosamine pH 7.5, 37°C Rattus norvegicus
5.1.3.14 0.026
-
 UDP-N-acetyl-D-glucosamine 37°C, pH 7.5 Rattus norvegicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.1.3.14 additional information Rattus norvegicus the bifunctional enzyme UDP-N-acetylglucosamine 2-epimerase/ManNAc kinase catalyzes the first two steps in the biosynthesis of the sialic acids ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.183 Rattus norvegicus
-
-
-
5.1.3.14 Rattus norvegicus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.183 using a single ion exchange chromatographic step. The resulting protein is estimated to be 80% pure Rattus norvegicus
5.1.3.14 recombinant enzyme expressed in Spodoptera frugiperda cells using a baculovirus expression system Rattus norvegicus

Reaction

EC Number Reaction Comment Organism Reaction ID
3.2.1.183 UDP-N-acetyl-alpha-D-glucosamine + H2O = N-acetyl-D-mannosamine + UDP the epimerase reaction is shown to proceed with a retention of stereochemistry at C-1, and the loss of UDP is found to occur via a C-O bond cleavage process. Results support a mechanism involving an anti-elimination of UDP followed by the syn-hydration of 2-acetamidoglucal Rattus norvegicus
a

Storage Stability

EC Number Storage Stability Organism
3.2.1.183 4°C, limited stability upon storage at 4 °C. The enzymatic activity is lost upon centrifugal concentration using ultrafiltration Rattus norvegicus
5.1.3.14 4°C, purified enzyme is 80% pure, no further purification because it is unstable to freezing and has limited stability upon storage at 4°C Rattus norvegicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.183 UDP-N-acetyl-alpha-D-glucosamine + H2O
-
 Rattus norvegicus N-acetyl-alpha-D-mannosamine + UDP
-
 ?
5.1.3.14 additional information reaction mechanism involving an anti-elimination of UDP to give 2-acetamidoglucal, followed by a syn-addition of water Rattus norvegicus ?
-
 ?
5.1.3.14 additional information the bifunctional enzyme UDP-N-acetylglucosamine 2-epimerase/ManNAc kinase catalyzes the first two steps in the biosynthesis of the sialic acids Rattus norvegicus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.183 UDP-N-acetylglucosamine 2-epimerase
-
 Rattus norvegicus
5.1.3.14 More bifunctional enzyme UDP-N-acetylglucosamine 2-epimerase/ManNAc kinase Rattus norvegicus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.183 37
-
 assay at Rattus norvegicus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.183 0.33
-
 UDP-N-acetyl-alpha-D-glucosamine pH 7.5, 37°C Rattus norvegicus
5.1.3.14 0.33
-
 UDP-N-acetyl-D-glucosamine 37°C, pH 7.5 Rattus norvegicus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.183 7.5
-
 assay at Rattus norvegicus