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Information on EC 1.1.1.B65 - (R)-mandelate dehydrogenase [NAD(P)+]
for references in articles please use BRENDA:EC1.1.1.B65
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preliminary BRENDA-supplied EC number
EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.B65 (R)-mandelate dehydrogenase [NAD(P)+]
The expected taxonomic range for this enzyme is: Pseudomonas putida
Synonyms
RMDH, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
RMDH
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SYSTEMATIC NAME
IUBMB Comments
(R)-mandelate:NAD(P)+ 2-oxidoreductase
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-mandelate + NAD+
phenylglyoxylate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
(R)-mandelate + NAD+
phenylglyoxylate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
(R)-mandelate + NADP+
phenylglyoxylate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
(R)-mandelate + NADP+
phenylglyoxylate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-mandelate + NAD+
phenylglyoxylate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
(R)-mandelate + NAD+
phenylglyoxylate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
-
inhibits the enzyme activity about 68% and 89% in the concentration of 10 mM and 50 mM,respectively
Triton X-100
-
0.25% of TritonX-100 has slight improvement on enzyme activity, whereas 0.75% of TritonX-100 slightly inhibits the enzyme activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
DTT
-
enhancement of enzyme activity of 26% and 33% in the concentration of 10 mM and 50 mM
Triton X-100
-
0.25% of TritonX-100 has slight improvement on enzyme activity, whereas 0.75% of TritonX-100 slightly inhibits the enzyme activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from soil around the schoolyard of Nanjing University of Science and Technology (Nanjing, China)
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-
brenda
isolated from soil around the schoolyard of Nanjing University of Science and Technology (Nanjing, China)
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-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
-
purified enzyme, the stability drops significantly at pH 8.5 and pH 9.0, the enzyme loses 85% and 94% of the activity when incubated for 3.5 h at 30°C, and it loses 11% of activity at pH 6.0 after 3.5 h at 30°C. After 96 h at 4°C, 78% of enzyme activity is retained at pH 6.0, and 30% at pH 8.5
743100
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
purified enzyme, pH 8.5, 31% activity remaining after 0.5 h, and 20% after 1 h
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, purified enzyme, 96 h, 78% of enzyme activity is retained at pH 6.0, and 30% at pH 8.5
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 11fold by ammonium sulfate fractionation and hydrophobic interaction chromatography
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang, J.; Feng, J.; Li, W.; Yang, C.; Chen, X.; Bao, B.; Yang, J.; Wang, P.; Li, D.; Shi, R.
Characterization of a novel (R)-mandelate dehydrogenase from Pseudomonas putida NUST506
J. Mol. Catal. B
120
23-27
2015
Pseudomonas putida, Pseudomonas putida NUST506
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brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.B65)
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Release 2023.1 (January 2023)
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