Any feedback?
Information on EC 1.1.1.67 - mannitol 2-dehydrogenase and Organism(s) Pseudomonas fluorescens and UniProt Accession O08355
for references in articles please use BRENDA:EC1.1.1.67Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.1.1.67 mannitol 2-dehydrogenaseSpecify your search results
Word Map
- 1.1.1.67
-
polyol
- fluorescens
- d-fructose
- synthesis
-
5-dehydrogenase
-
1.1.1.138
-
heterofermentative
- reuteri
- gluconobacter
- industry
- pfldh
- arabitol
- molasses
- nutrition
- biotechnology
- analysis
The taxonomic range for the selected organisms is: Pseudomonas fluorescens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
pfmdh, mannitol 2-dehydrogenase, mannitol-2-dehydrogenase, nadh-dependent mannitol dehydrogenase, nad+-dependent mannitol dehydrogenase, psm2dh, tm0298, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-mannitol dehydrogenase
mannitol dehydrogenase
-
-
-
-
D-mannitol dehydrogenase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-mannitol + NAD+ = D-fructose + NADH + H+
the oxyanion hole of mannitol 2-dehydrogenase drives a precatalytic conformational equilibrium at the ternary complex level in which the reactive group of the substrate is activated for chemical conversion through its precise alignment with the unprotonated side chain of Lys295 in mannitol oxidation and C=O bond polarization by the carboxamide moieties of Asn191 and Asn300 in fructose reduction. In the subsequent hydride transfer step, the two asparagine residues provide about 40 kJ/mol of electrostatic stabilization
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
D-mannitol:NAD+ 2-oxidoreductase
-
CAS REGISTRY NUMBER
COMMENTARY
9001-65-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-mannitol + NAD+
D-fructose + NADH + H+
wild-type enzyme
-
-
r
D-fructose + NADH + H+
D-mannitol + NAD+
-
Asn300 has an auxiliary role in stabilization of the transition state of hydride transfer and His303 contributes to substrate positioning, role of Lys295 in general base enzymic catalysis
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
the epsilon-NH2 group of Lys295 participates in an obligatory pH-dependent, pre-catalytic equilibrium which may control alcohol/alkoxide equilibration of the enzyme-bound D-mannitol and activates the C2 atom for subsequent catalytic oxidation by NAD+
-
-
?
additional information
?
-
no activity with glycerol, 1, 2-hexanediol, and 1,2,3-hexanetriol
-
-
?
additional information
?
-
-
no activity with glycerol, 1, 2-hexanediol, and 1,2,3-hexanetriol
-
-
?
additional information
?
-
-
among the Escherichia coli strains, BL21 (DE3) plysS exhibits the maximum expression level of MDH (11mg/L)
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-mannitol + NAD+
D-fructose + NADH + H+
wild-type enzyme
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADP+
400fold preference of the enzyme for NAD+ as compared to NADP+
NAD+
binding structure, the carboxylate group of Asp69 forms a bifurcated hydrogen bond with the 2' and 3' hydroxyl groups of the adenosine of NAD+ and contributes to the 400fold preference of the enzyme for NAD+ as compared to NADP+, overview
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
no inhibition of M2DH by bovine serum albumin
-
additional information
-
no inhibition of M2DH by bovine serum albumin
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
no activation of M2DH by bovine serum albumin
-
additional information
-
no activation of M2DH by bovine serum albumin
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
33.15
D-arabitol
mutant enzyme H303A/R73A/K381A, at pH 7.4 and 25°C
0.24
D-fructose
wild-type, pH 7.1, temperature not specified in the publication
0.54
D-fructose
mutant N191D, pH 10.0, temperature not specified in the publication
3.9
D-fructose
mutant N300D, pH 10.0, temperature not specified in the publication
6
D-fructose
mutant N191D, pH 7.1, temperature not specified in the publication
20
D-fructose
mutant N191D/N300D, pH 10.0, temperature not specified in the publication
22
D-fructose
mutant N300D, pH 6.8, temperature not specified in the publication
0.3
D-mannitol
mutant N300D, pH 10.0, temperature not specified in the publication
0.32
D-mannitol
mutant N191D, pH 10.0, temperature not specified in the publication
8.15
D-mannitol
mutant enzyme H303A/R73A/K381A, at pH 7.4 and 25°C
9
D-mannitol
mutant N191D, pH 7.1, temperature not specified in the publication
21
D-mannitol
wild-type, pH 7.1, temperature not specified in the publication
93
D-mannitol
mutant N300D, pH 6.8, temperature not specified in the publication
1800
meso-erythritol
Km far above 1800 mM, mutant enzyme E133A, at pH 7.4 and 25°C
1800
meso-erythritol
Km far above 1800 mM, mutant enzyme E133Q, at pH 7.4 and 25°C
1800
meso-erythritol
Km far above 1800 mM, mutant enzyme H303A, at pH 7.4 and 25°C
1800
meso-erythritol
Km far above 1800 mM, mutant enzyme N191A, at pH 7.4 and 25°C
1800
meso-erythritol
Km far above 1800 mM, mutant enzyme N300A, at pH 7.4 and 25°C
1800
meso-erythritol
Km far above 1800 mM, mutant enzyme N300S, at pH 7.4 and 25°C
1800
meso-erythritol
Km far above 1800 mM, wild type enzyme, at pH 7.4 and 25°C
0.001
NAD+
mutant N300D, pH 6.8, temperature not specified in the publication
0.054
NAD+
mutant N191D, pH 10.0, temperature not specified in the publication
0.074
NAD+
mutant N300D, pH 10.0, temperature not specified in the publication
0.231
NAD+
mutant N191D, pH 7.1, temperature not specified in the publication
0.775
NAD+
wild-type, pH 7.1, temperature not specified in the publication
0.008
NADH
mutant N191D, pH 7.1, temperature not specified in the publication
0.009
NADH
mutant N300D, pH 10.0, temperature not specified in the publication
0.011
NADH
mutant N191D/N300D, pH 10.0, temperature not specified in the publication
0.016
NADH
mutant N191D, pH 10.0, temperature not specified in the publication
0.02
NADH
mutant N300D, pH 6.8, temperature not specified in the publication
0.067
NADH
wild-type, pH 7.1, temperature not specified in the publication
additional information
additional information
kinetic modeling
-
additional information
additional information
steady-state kinetic analysis, recombinant wild-type and mutant enzymes, overview
-
additional information
additional information
-
steady-state kinetic analysis, recombinant wild-type and mutant enzymes, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0017
D-arabitol
mutant enzyme H303A/R73A/K381A, at pH 7.4 and 25°C
0.15
D-fructose
mutant N191D/N300D, pH 10.0, temperature not specified in the publication
0.8
D-fructose
mutant N300D, pH 10.0, temperature not specified in the publication
0.9
D-fructose
mutant N300D, pH 6.8, temperature not specified in the publication
2.7
D-fructose
mutant N191D, pH 7.1, temperature not specified in the publication
8.2
D-fructose
mutant N191D, pH 10.0, temperature not specified in the publication
61
D-fructose
wild-type, pH 7.1, temperature not specified in the publication
0.00055
D-mannitol
mutant N191D, pH 7.1, temperature not specified in the publication
0.001
D-mannitol
mutant enzyme H303A/R73A/K381A, at pH 7.4 and 25°C
0.0011
D-mannitol
mutant N191D, pH 10.0, temperature not specified in the publication
0.0014
D-mannitol
mutant N300D, pH 6.8, temperature not specified in the publication
0.0015
D-mannitol
mutant N300D, pH 10.0, temperature not specified in the publication
15.9
D-mannitol
wild-type, pH 7.1, temperature not specified in the publication
0.0012
meso-erythritol
mutant enzyme N191A, at pH 7.4 and 25°C
0.0024
meso-erythritol
mutant enzyme N300S, at pH 7.4 and 25°C
0.0036
meso-erythritol
mutant enzyme N300A, at pH 7.4 and 25°C
0.0159
meso-erythritol
mutant enzyme H303A, at pH 7.4 and 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000051
D-arabitol
mutant enzyme H303A/R73A/K381A, at pH 7.4 and 25°C
0.0074
D-fructose
mutant N191D/N300D, pH 10.0, temperature not specified in the publication
0.041
D-fructose
mutant N300D, pH 6.8, temperature not specified in the publication
0.205
D-fructose
mutant N300D, pH 10.0, temperature not specified in the publication
0.45
D-fructose
mutant N191D, pH 7.1, temperature not specified in the publication
15
D-fructose
mutant N191D, pH 10.0, temperature not specified in the publication
250
D-fructose
wild-type, pH 7.1, temperature not specified in the publication
0.000015
D-mannitol
mutant N300D, pH 6.8, temperature not specified in the publication
0.000061
D-mannitol
mutant N191D, pH 7.1, temperature not specified in the publication
0.00016
D-mannitol
mutant enzyme H303A/R73A/K381A, at pH 7.4 and 25°C
0.0034
D-mannitol
mutant N191D, pH 10.0, temperature not specified in the publication
0.0049
D-mannitol
mutant N300D, pH 10.0, temperature not specified in the publication
0.757
D-mannitol
wild-type, pH 7.1, temperature not specified in the publication
0.0000021
meso-erythritol
mutant enzyme N191A, at pH 7.4 and 25°C
0.0000044
meso-erythritol
mutant enzyme N300S, at pH 7.4 and 25°C
0.0000065
meso-erythritol
mutant enzyme N300A, at pH 7.4 and 25°C
0.000029
meso-erythritol
mutant enzyme H303A, at pH 7.4 and 25°C
0.00088
meso-erythritol
mutant enzyme E133Q, at pH 7.4 and 25°C
0.00097
meso-erythritol
mutant enzyme E133A, at pH 7.4 and 25°C
0.0024
NAD+
mutant N191D, pH 7.1, temperature not specified in the publication
0.02
NAD+
mutant N191D, pH 10.0, temperature not specified in the publication
0.02
NAD+
mutant N300D, pH 10.0, temperature not specified in the publication
1.4
NAD+
mutant N300D, pH 6.8, temperature not specified in the publication
20
NAD+
wild-type, pH 7.1, temperature not specified in the publication
15
NADH
mutant N191D/N300D, pH 10.0, temperature not specified in the publication
45
NADH
mutant N300D, pH 6.8, temperature not specified in the publication
89
NADH
mutant N300D, pH 10.0, temperature not specified in the publication
340
NADH
mutant N191D, pH 7.1, temperature not specified in the publication
510
NADH
mutant N191D, pH 10.0, temperature not specified in the publication
910
NADH
wild-type, pH 7.1, temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.003
NAD+
mutant N191D, pH 7.1, temperature not specified in the publication
0.07
NAD+
mutant N300D, pH 6.8, temperature not specified in the publication
0.08
NAD+
wild-type, pH 7.1, temperature not specified in the publication
0.061
NADH
mutant N300D, pH 6.8, temperature not specified in the publication
0.064
NADH
mutant N191D, pH 7.1, temperature not specified in the publication
0.08
NADH
wild-type, pH 7.1, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
63
-
MDH expressed in Escherichia coli strain BL21 (DE3) plysS, with fructose as substrate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
54000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, binary complex of selenomethionine substituted proteins with NAD(H) and a ternary complex with NAD(H) and D-mannitol have been determined to resolutions of 1.7 and 1.8 A respectively
-
hanging drop vapor diffusion method, binary complex with NAD+ and ternary complex with NAD+ and D-mannitol have been determined to resolutions of 1.7 and 1.8 A and R-factors of 0.171 and 0.176 respectively
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D230A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
D69A
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
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
H303A/R373A/K381A
the mutant shows severely reduced catalytic efficiency compared to 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 enzymeNAD+-mannitol complex
N300A
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
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
H303A
-
mutant enzyme displays catalytic efficiency for NAD+-dependent oxidation of D-mannitol 300fold below the wild-type value
K295A
K295M
-
2000000fold lower turnover number for D-mannitol oxidation at pH 10.0 than the wild-type enzyme
N300A
-
mutant enzyme displays catalytic efficiency for NAD+-dependent oxidation of D-mannitol 1000fold below the wild-type value
additional information
application of a modular screening procedure that can identify the optimal operating policy of an enzymatic reactor, which minimizes the enzyme consumption, given the process kinetic model, and an imposed production capacity. Following an optimization procedure, the process effectiveness is evaluated in a systematic approach, by including simple batch reactor (BR), batch with intermittent addition of the key-enzyme following certain optimal policies (BRP). The enzymatic reduction of D-fructose to mannitol is used as a model system utilizing suspended MDH (mannitol dehydrogenase) and NADH (nicotinamide adenine dinucleotide) cofactor, with the in-situ continuous regeneration of the cofactor by the expense of formate degradation in the presence of suspended FDH (formate dehydrogenase). The NADH-dependent FDH and MDH typical activity in D-fructose reduction is of 1-2 U/ml in a batch reactor
D69A
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 equally utilized as NAD(H)
D69A
utilizes NAD(H) and NADP(H) with similar catalytic efficiencies. Uses NADP(H) almost as well as wild-type enzyme uses NAD(H)
N191A
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 enzymeNAD+-mannitol complex
N191A
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
N300D
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
N300D
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
K295A
-
30000fold lower turnover number for D-mannitol oxidation at pH 10.0 than the wild-type enzyme
K295A
-
mutant enzyme displays catalytic efficiency for NAD+-dependent oxidation of D-mannitol 400000fold below the wild-type value
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
histidine-tagged recombinant protein, expressed in Escherichia coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant enzymes in Escherichia coli strain JM109
gene mtlD, recombinant overexpression of the enzyme in Escherichia coli strain JM109
expression of wild-type enzyme and mutant enzymes in Escherichia coli
-
subcloned into vector pDEST110 and overexpressed in different strains of Escherichia coli (BL21 (DE3) plysS, JM109, Origami(DE3) or M15)
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
industry
redox balancing between the intracellular NADP(H) and NAD(H) based on NAD(P)(H)-dependent interconversion of mannitol and fructose by M2DH may be a useful strategy of metabolic engineering
synthesis
mannitol is a natural hexitol with important applications in medicine and food industry. Development of a production method on an industrial scale, optimization and evaluation of production in a batch reactor (BR, or BRP operation) for a complex bi-enzymatic system with suspended enzymes and cofactor regeneration, method modeling, molecular calculations and simulations, detailed overview
industry
-
best strain for expression of MDH in both laboratory and industrial applications is Escherichia coli BL21 (DE3) plysS
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yamanaka, K.; Sakai, S.
Production of polyol dehydrogenases in bacteria
Can. J. Microbiol.
14
391-396
1968
Lactobacillus gayonii, Lactobacillus pentoaceticus, Leuconostoc mesenteroides, Levilactobacillus brevis, Pseudomonas aeruginosa, Pseudomonas coronafaciens, Pseudomonas fluorescens, Sarcina aurantiaca, Sarcina marginata
Slatner, M.; Nagl, G.; Haltrich, D.; Kulbe, K.D.; Nidetzky, B.
Enzymic synthesis of mannitol: reaction engineering for a recombinant mannitol dehydrogenase
Ann. N. Y. Acad. Sci.
864
450-453
1998
Pseudomonas fluorescens
Slatner, M.; Nidetzky, B.; Kulbe, K.D.
Kinetic study of the catalytic mechanism of mannitol dehydrogenase from Pseudomonas fluorescens
Biochemistry
38
10489-10498
1999
Pseudomonas fluorescens
Brunker, P.; Altenbuchner, J.; Kulbe, K.D.; Mattes, R.
Cloning, nucleotide sequence and expression of a mannitol dehydrogenase gene from Pseudomonas fluorescens DSM 50106 in Escherichia coli
Biochim. Biophys. Acta
1351
157-167
1997
Pseudomonas fluorescens
Klimacek, M.; Nidetzky, B.
A catalytic consensus motif for D-mannitol 2-dehydrogenase, a member of a polyol-specific long-chain dehydrogenase family, revealed by kinetic characterization of site-directed mutants of the enzyme from Pseudomonas fluorescens
Biochem. J.
367
13-18
2002
Pseudomonas fluorescens
Klimacek, M.; Kavanagh, K.L.; Wilson, D.K.; Nidetzky, B.
On the role of Bronsted catalysis in Pseudomonas fluorescens mannitol 2-dehydrogenase
Biochem. J.
375
141-149
2003
Pseudomonas fluorescens
Kavanagh, K.L.; Klimacek, M.; Nidetzky, B.; Wilson, D.K.
Crystal structure of Pseudomonas fluorescens mannitol 2-dehydrogenase: evidence for a very divergent long-chain dehydrogenase family
Chem. Biol. Interact.
143-144
551-558
2003
Pseudomonas fluorescens
Kavanagh, K.L.; Klimacek, M.; Nidetzky, B.; Wilson, D.K.
Crystal structure of Pseudomonas fluorescens mannitol 2-dehydrogenase binary and ternary complexes. Specificity and catalytic mechanism
J. Biol. Chem.
277
43433-43442
2002
Pseudomonas fluorescens
Klimacek, M.; Nidetzky, B.
Examining the relative timing of hydrogen abstraction steps during NAD+-dependent oxidation of secondary alcohols catalyzed by long-chain D-mannitol dehydrogenase from Pseudomonas fluorescens using pH and kinetic isotope effects
Biochemistry
41
10158-10165
2002
Pseudomonas fluorescens
Bubner, P.; Klimacek, M.; Nidetzky, B.
Structure-guided engineering of the coenzyme specificity of Pseudomonas fluorescens mannitol 2-dehydrogenase to enable efficient utilization of NAD(H) and NADP(H)
FEBS Lett.
582
233-237
2008
Pseudomonas fluorescens (O08355), Pseudomonas fluorescens
Haghighatian, M.; Mofid, M.R.; Nekouei, M.K.; Yaghmaei, P.; Tafreshi, A.H.
Isomalt production by cloning, purifying and expressing of the MDH gene from Pseudomonas fluorescens DSM 50106 in different strains of E. coli
Pak. J. Biol. Sci.
11
2001-2006
2008
Pseudomonas fluorescens
Klimacek, M.; Nidetzky, B.
The oxyanion hole of Pseudomonas fluorescens mannitol 2-dehydrogenase: a novel structural motif for electrostatic stabilization in alcohol dehydrogenase active sites
Biochem. J.
425
455-463
2010
Pseudomonas fluorescens (O08355), Pseudomonas fluorescens
Klimacek, M.; Nidetzky, B.
From alcohol dehydrogenase to a "one-way" carbonyl reductase by active-site redesign: a mechanistic study of mannitol 2-dehydrogenase from Pseudomonas fluorescens
J. Biol. Chem.
285
30644-30653
2010
Pseudomonas fluorescens (O08355), Pseudomonas fluorescens
Klimacek, M.; Brunsteiner, M.; Nidetzky, B.
Dynamic mechanism of proton transfer in mannitol 2-dehydrogenase from Pseudomonas fluorescens: mobile GLU292 controls proton relay through a water channel that connects the active site with bulk solvent
J. Biol. Chem.
287
6655-6667
2012
Pseudomonas fluorescens (O08355), Pseudomonas fluorescens
Lucas, J.; Siegel, J.
Erratum: Quantitative functional characterization of conserved molecular interactions in the active site of mannitol 2-dehydrogenase
Protein Sci.
24
936-945
2015
Pseudomonas fluorescens (O08355), Pseudomonas fluorescens
Crisan, M.; Maria, G.
Modular simulation to determine the optimal operating policy of a batch reactor for the enzymatic fructose reduction to mannitol with the in situ continuous enzymatic regeneration of the NAD cofactor
Rev. Chim.
68
2196-2203
2017
Pseudomonas fluorescens (O08355), Pseudomonas fluorescens DSM 50106 (O08355)
-
EXTERNAL LINKS (specific for EC-Number 1.1.1.67)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
