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Literature summary extracted from

  • Sand, M.; Rodrigues, M.; Gonzalez, J.M.; de Crecy-Lagard, V.; Santos, H.; Mueller, V.; Averhoff, B.
    Mannitol-1-phosphate dehydrogenases/phosphatases: a family of novel bifunctional enzymes for bacterial adaptation to osmotic stress (2015), Environ. Microbiol., 17, 711-719.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.17 gene mtlD, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis Acinetobacter baylyi
3.1.3.22 gene mtlD, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis Acinetobacter baylyi

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.22 NaF complete inhibition Acinetobacter baylyi
3.1.3.22 Sodium fluoride complete inhibition at 1 mM Acinetobacter baylyi

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.3.22 Ca2+ stimulates activity but not as efficient as Mg2+ Acinetobacter baylyi
3.1.3.22 Ca2+ activates the phosphatase activity, 14% activation compared to Mg2+ Acinetobacter baylyi
3.1.3.22 Cu2+ stimulates activity but not as efficient as Mg2+ Acinetobacter baylyi
3.1.3.22 Cu2+ activates phosphatase activity, 15% activation compared to Mg2+ Acinetobacter baylyi
3.1.3.22 Mg2+ phosphatase activity is strictly Mg2+ dependent with maximum activity at 5 mM Acinetobacter baylyi
3.1.3.22 Mg2+ the enzyme's phosphatase activity is strictly Mg2+ dependent, maximal activity with MgCl2, 91% with MgSO4 Acinetobacter baylyi
3.1.3.22 Zn2+ stimulates activity but not as efficient as Mg2+ Acinetobacter baylyi
3.1.3.22 Zn2+ activates the phosphatase activity, 30% activation compared to Mg2+ Acinetobacter baylyi

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.17 D-mannitol 1-phosphate + NADP+ Acinetobacter baylyi
-
 D-fructose 6-phosphate + NADPH + H+
-
 r
1.1.1.17 D-mannitol 1-phosphate + NADP+ Acinetobacter baylyi ATCC 33305
-
 D-fructose 6-phosphate + NADPH + H+
-
 r
1.1.1.17 additional information Acinetobacter baylyi MtlD is a bifunctional enzyme of mannitol biosynthesis that combines mannitol-1-phosphate dehydrogenase and phosphatase activities in a single polypeptide chain ?
-
 ?
1.1.1.17 additional information Acinetobacter baylyi ATCC 33305 MtlD is a bifunctional enzyme of mannitol biosynthesis that combines mannitol-1-phosphate dehydrogenase and phosphatase activities in a single polypeptide chain ?
-
 ?
3.1.3.22 D-mannitol 1-phosphate + H2O Acinetobacter baylyi
-
 D-mannitol + phosphate
-
 ?
3.1.3.22 mannitol 1-phosphate + H2O Acinetobacter baylyi
-
 mannitol + phosphate
-
 ?
3.1.3.22 mannitol 1-phosphate + H2O Acinetobacter baylyi ATCC 33305
-
 mannitol + phosphate
-
 ?
3.1.3.22 additional information Acinetobacter baylyi MtlD is a bifunctional enzyme of mannitol biosynthesis that combines mannitol-1-phosphate dehydrogenase and phosphatase activities in a single polypeptide chain ?
-
 ?
3.1.3.22 additional information Acinetobacter baylyi ATCC 33305 MtlD is a bifunctional enzyme of mannitol biosynthesis that combines mannitol-1-phosphate dehydrogenase and phosphatase activities in a single polypeptide chain ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.17 Acinetobacter baylyi Q6FBP5
-
-
1.1.1.17 Acinetobacter baylyi ATCC 33305 Q6FBP5
-
-
3.1.3.22 Acinetobacter baylyi
-
-
-
3.1.3.22 Acinetobacter baylyi Q6FBP5
-
-
3.1.3.22 Acinetobacter baylyi ATCC 33305 Q6FBP5
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.3.22 103
-
 enzyme in presence of 5 mM MgSO4, pH 6.5, 30°C Acinetobacter baylyi

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.17 D-mannitol 1-phosphate + NADP+
-
 Acinetobacter baylyi D-fructose 6-phosphate + NADPH + H+
-
 r
1.1.1.17 D-mannitol 1-phosphate + NADP+
-
 Acinetobacter baylyi ATCC 33305 D-fructose 6-phosphate + NADPH + H+
-
 r
1.1.1.17 additional information MtlD is a bifunctional enzyme of mannitol biosynthesis that combines mannitol-1-phosphate dehydrogenase and phosphatase activities in a single polypeptide chain Acinetobacter baylyi ?
-
 ?
1.1.1.17 additional information MtlD is a bifunctional enzyme of mannitol biosynthesis that combines mannitol-1-phosphate dehydrogenase and phosphatase activities in a single polypeptide chain Acinetobacter baylyi ATCC 33305 ?
-
 ?
3.1.3.22 4-nitrophenyl phosphate + H2O
-
 Acinetobacter baylyi 4-nitrophenol + phosphate
-
 ?
3.1.3.22 D-mannitol 1-phosphate + H2O
-
 Acinetobacter baylyi D-mannitol + phosphate
-
 ?
3.1.3.22 mannitol 1-phosphate + H2O
-
 Acinetobacter baylyi mannitol + phosphate
-
 ?
3.1.3.22 mannitol 1-phosphate + H2O
-
 Acinetobacter baylyi ATCC 33305 mannitol + phosphate
-
 ?
3.1.3.22 additional information substrates such as fructose 6-phosphate, ribose 5-phosphate, glucose 6-phosphate and glucose 1-phosphate are not dephosphorylated Acinetobacter baylyi ?
-
 ?
3.1.3.22 additional information MtlD is a bifunctional enzyme of mannitol biosynthesis that combines mannitol-1-phosphate dehydrogenase and phosphatase activities in a single polypeptide chain Acinetobacter baylyi ?
-
 ?
3.1.3.22 additional information MtlD is a bifunctional enzyme of mannitol biosynthesis that combines mannitol-1-phosphate dehydrogenase and phosphatase activities in a single polypeptide chain Acinetobacter baylyi ATCC 33305 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.1.17 mannitol-1-phosphate dehydrogenase
-
 Acinetobacter baylyi
1.1.1.17 Mtl-1-P dehydrogenase
-
 Acinetobacter baylyi
1.1.1.17 MtlD
-
 Acinetobacter baylyi
3.1.3.22 mannitol-1-phosphatase
-
 Acinetobacter baylyi
3.1.3.22 mannitol-1-phosphate dehydrogenases/phosphatase
-
 Acinetobacter baylyi
3.1.3.22 MtlD
-
 Acinetobacter baylyi
3.1.3.22 MtlD a bifunctional enzyme that combines mannitol-1-phosphate dehydrogenase and phosphatase activities Acinetobacter baylyi

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.3.22 30
-
 assay at Acinetobacter baylyi

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.3.22 5
-
-
 Acinetobacter baylyi

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.3.22 4.5 6 the enzyme retains activity of 60% at pH 6.0 and 47% at pH 4.5, respectively Acinetobacter baylyi
3.1.3.22 4.7 6 60% of maximal activity at pH 6.0 and 47% at pH 4.5 Acinetobacter baylyi

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.17 NADP+
-
 Acinetobacter baylyi
1.1.1.17 NADPH
-
 Acinetobacter baylyi

General Information

EC Number General Information Comment Organism
1.1.1.17 evolution the C-terminus of MtlD from Acinetobacter baylyi is similar to dehydrogenase domains found in other dehydrogenases with a glycine-rich conserved domain (Rossmann-fold) starting at position 247 for cosubstrate binding (GIHGFGAIGGG). The N-terminal domain of MtlD is similar to members of the HAD (haloacid dehalogenase) superfamily Acinetobacter baylyi
1.1.1.17 metabolism mannitol-1-phosphate dehydrogenase MtlD is essential for mannitol biosynthesis and catalyses the first step in mannitol biosynthesis, the reduction of fructose-6-phosphate to the intermediate mannitol-1-phosphate Acinetobacter baylyi
1.1.1.17 physiological function the nutritionally versatile soil bacterium Acinetobacter baylyi ADP1 copes with salt stress by the accumulation of compatible solutes. The bacterium synthesizes the sugar alcohol mannitol de novo in response to osmotic stress. THe enzyme is essential for mannitol 1-phosphate biosynthesis, and it also possesses a unique sequence among known mannitol-1-phosphate dehydrogenases with a haloacid dehalogenase (HAD)-like phosphatase domain at the N-terminus. This domain has phosphatase activity Acinetobacter baylyi
3.1.3.22 evolution the C-terminus of MtlD from Acinetobacter baylyi is similar to dehydrogenase domains found in other dehydrogenases with a glycine-rich conserved domain (Rossmann-fold) starting at position 247 for cosubstrate binding (GIHGFGAIGGG). The N-terminal domain of MtlD is similar to members of the HAD (haloacid dehalogenase) superfamily Acinetobacter baylyi
3.1.3.22 physiological function the nutritionally versatile soil bacterium Acinetobacter baylyi ADP1 copes with salt stress by the accumulation of compatible solutes. The bacterium synthesizes the sugar alcohol mannitol de novo in response to osmotic stress. THe enzyme is essential for mannitol 1-phosphate biosynthesis, and it also possesses a unique sequence among known mannitol-1-phosphate dehydrogenases with a haloacid dehalogenase (HAD)-like phosphatase domain at the N-terminus. This domain has phosphatase activity Acinetobacter baylyi