Species: Petroselinum crispum
The enzyme catalyzing the convertion of nicotinate to its N-glucosyl conjugate has been partially purified from cell cultures of Petroselinum crispum. N-glucosylnicotinate was proposed to serve as a storage compound supported by the corresponding enzyme activity being present during the entire growth circle and the relatively short half life of about 24 hours. The enzyme, i.e. UDPG:nicotinate N-glucosyltransferase has been shown to promote free reversibility of the reaction indicating a point of regulation for the pyridine nucleotide cycling in plants and highlights the high group-transfer potential of N-glucosylnicotinate [Upmeier88].
Molecular Weight of Polypeptide: 46 kD (experimental) [Upmeier88]
EC Number: 188.8.131.52UDP-α-D-glucose + nicotinate ⇄ N-glucosylnicotinate + UDP
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction of enzyme catalysis.
This reaction is reversible.
In Pathways: N-glucosylnicotinate metabolismInhibitors (Unknown Mechanism): Zn2+ [Upmeier88], p-chloromercuribenzoateKinetic Parameters:
T(opt): 30 °C [Upmeier88]
pH(opt): 7.8-8.2 [Upmeier88]
Upmeier88: Upmeier B, Thomzik JE, Barz W (1988). "Enzymatic studies on the reversible synthesis of nicotinic acid-N-glucoside in heterotrophic parsley cell suspension cultures." Z. Naturforsch. 43c, 835-842.
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