1.1.1.379: (R)-mandelate dehydrogenase

This is an abbreviated version!
For detailed information about (R)-mandelate dehydrogenase, go to the full flat file.

Reaction

Synonyms

D(-)-mandelate dehydrogenase, D-mandelate dehydrogenase, D-ManDH, D-ManDH2, DMDH, LhDMDH, ManDH2, NAD+-dependent D-mandelate dehydrogenase, NAD-dependent D-mandelate dehydrogenase

ECTree

     1 Oxidoreductases

         1.1 Acting on the CH-OH group of donors

             1.1.1 With NAD⁺ or NADP⁺ as acceptor

                1.1.1.379 (R)-mandelate dehydrogenase

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Results	in table
2	AA Sequence
1	Application
2	Cloned(Commentary)
5	Cofactor
2	Crystallization (Commentary)
2	General Information
23	Inhibitors
2	kcat/KM [mM/s]
3	Ki Value [mM]
13	KM Value [mM]
1	Metals/Ions
2	Molecular Weight [Da]
3	Natural Substrates/ Products (Substrates)
6	Organism
6	pH Optimum
4	pH Stability
1	pI Value
1	Protein Variants
3	Purification (Commentary)
1	Reaction
6	Reference
2	Specific Activity [micromol/min/mg]
15	Substrates and Products (Substrate)
4	Subunits
13	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]
1	Temperature Range [°C]
1	Temperature Stability [°C]
2	Turnover Number [1/s]

Engineering

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Engineering on EC 1.1.1.379 - (R)-mandelate dehydrogenase

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

additional information

Schleiferilactobacillus harbinensis

A0A5P8Q188

by coculturing two Escherichia coli strains expressing LhDMDH and lactate dehydrogenase (LDH) from Lactobacillus casei, LcLDH, a system for the efficient synthesis of phenylglyoxylic acid (PGA) is developed, achieving a 60% theoretical yield and 99% purity without adding coenzyme or cosubstrate. Implementation of a promising strategy for the chiral resolution of racemic mandelic acid and the biosynthesis of PGA. Whole cell catalysis is a preferred option to eliminate the influence of low thermostability of enzyme LhDMDH in the biosynthesis of PGA

763170