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Native Pyruvate decarboxylase from Thermophillic bacteria

Cat No.
NATE-1159
Description
Pyruvate decarboxylase (PDC) is a homotetrameric enzyme that catalyses the decarboxylation of pyruvic acid to acetaldehyde and carbon dioxide in the cytoplasm. Pyruvate decarboxylase depends on cofactors thiamine pyrophosphate (TPP) and magnesium. PDC contains a β-α-β structure, yielding parallel β-sheets.
Abbr
PDC, Native (Thermophillic bacteria)
Alias
PDC
Source
Thermophillic bacteria
Applications
C-C bond formation: ligation of two aldehyde molecules enantioselectively to 2-hydroxy ketones; preparation of (R)-phenylacetylcarbinol (PAC)
Form
Frozen Liquid
Enzyme Commission Number
EC 4.1.1.1
CAS No.
9001-04-1
Unit Definition
One unit is defined as the amount of enzyme oxidizing 1 µmol of NADH (ε340=6.22 mM-1 cm-1) per 1 minute using pyruvate as a substrate.
Optimum pH
6
Thermal stability
100% stability after 1 hour at 50°C
Storage
Store at -20°C
Buffer
20 mM Tris-HCl (pH 7.5), 20 mM KCl
Synonyms
Pyruvate decarboxylase; EC 4.1.1.1; α-carboxylase (ambiguous); pyruvic decarboxylase; α-ketoacid carboxylase; 2-oxo-acid carboxy-lyase; 9001-04-1; 2-Oxo-acid carboxy-lyase; PDC
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