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1.1.1.67: mannitol 2-dehydrogenase

This is an abbreviated version!
For detailed information about mannitol 2-dehydrogenase, go to the full flat file.

Word Map on EC 1.1.1.67

Reaction

D-mannitol
+
NAD+
=
D-fructose
 +
NADH
 +
H+

Synonyms

alcohol dehydrogenase, zinc-containing, D-mannitol dehydrogenase, M2DH, mannitol 2-dehydrogenase, mannitol dehydrogenase, mannitol-2-dehydrogenase, MDH, mt-dh, MtDH, MtlD, NAD+-dependent mannitol dehydrogenase, NADH-dependent mannitol dehydrogenase, pfMDH, polyol dehydrogenase, PsM2DH, TM0298, TM_0298

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.67 mannitol 2-dehydrogenase

Engineering

Engineering on EC 1.1.1.67 - mannitol 2-dehydrogenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D230A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E133A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E133Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E292A
mutation partially disrupts the catalytic cycle. Role for residue Glu292 as a gate in a water chain mechanism of proton translocation. Removal of gatekeeper control in the E292A mutant results in a selective, up to 120fold slowing down of microscopicsteps immediately preceding catalytic oxidation of mannitol, consistent with the notion that formation of the productive enzyme-NAD-mannitol complex is promoted by a corresponding position change of Glu292
E68K
site-directed mutagenesis, the mutant shows an altered cofactor specificity compared to the wild-type enzyme, which is switched to NADP(H), EC 1.1.1.138, NADP(H) is preferred by 10fold over NAD(H)
E68K/D69A
shows about a 10fold preference for NADP(H) over NAD(H), accompanied by a small decrease in catalytic efficiency for NAD(H)-dependent reactions as compared to wild-type enzyme
H303A
H303A/R373A/K381A
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
K295A
K295M
-
2000000fold lower turnover number for D-mannitol oxidation at pH 10.0 than the wild-type enzyme
K381A
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
N191A
N191A/N300A
the rate constants for the overall hydride transfer to and from C-2 of mannitol are selectively slowed, with additive effects in the double mutant
N191D
the internal equilibrium of enzyme-NADH-fructose and enzyme-NAD+-mannitol is altered 10000- to 100000fold from being balanced in the wild-type enzyme to favoring enzyme-NAD+-mannitol in the single site mutants, N191D and N300D. N191D and N300D appear to lose fructose binding affinity due to deprotonation of the respective Asp above apparent pK values of 5.3  0.1 and 6.3  0.2, respectively
N191D/N300D
mutant behaves as a slow fructose reductase at pH 5.2, lacking measurable activity for mannitol oxidation in the pH range 6.8-10
N191L
the rate constants for the overall hydride transfer to and from C-2 of mannitol are selectively slowed, between 540- and 2700fold. Partial disruption of the oxyanion hole in the single-site mutant causes an upshift, by about 1.2 pH units, in the kinetic pK of the catalytic acid-base Lys295 in the enzyme–NAD+-mannitol complex
N300A
N300D
N300S
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
R373A
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
additional information