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Literature summary for 3.1.3.22 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
Search for more literature for 3.1.3.22

Cloned(Commentary)

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

Inhibitors

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-mannitol 1-phosphate + H2O Acinetobacter baylyi
-
 D-mannitol + phosphate
-
 ?
mannitol 1-phosphate + H2O Acinetobacter baylyi
-
 mannitol + phosphate
-
 ?
mannitol 1-phosphate + H2O Acinetobacter baylyi ATCC 33305
-
 mannitol + phosphate
-
 ?
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 ?
-
 ?
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

Organism UniProt Comment Textmining
Acinetobacter baylyi
-
-
-
Acinetobacter baylyi Q6FBP5
-
-
Acinetobacter baylyi ATCC 33305 Q6FBP5
-
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl phosphate + H2O
-
 Acinetobacter baylyi 4-nitrophenol + phosphate
-
 ?
D-mannitol 1-phosphate + H2O
-
 Acinetobacter baylyi D-mannitol + phosphate
-
 ?
mannitol 1-phosphate + H2O
-
 Acinetobacter baylyi mannitol + phosphate
-
 ?
mannitol 1-phosphate + H2O
-
 Acinetobacter baylyi ATCC 33305 mannitol + phosphate
-
 ?
additional information substrates such as fructose 6-phosphate, ribose 5-phosphate, glucose 6-phosphate and glucose 1-phosphate are not dephosphorylated Acinetobacter baylyi ?
-
 ?
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 ?
-
 ?
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

Synonyms Comment Organism
mannitol-1-phosphatase
-
 Acinetobacter baylyi
mannitol-1-phosphate dehydrogenases/phosphatase
-
 Acinetobacter baylyi
MtlD
-
 Acinetobacter baylyi
MtlD a bifunctional enzyme that combines mannitol-1-phosphate dehydrogenase and phosphatase activities Acinetobacter baylyi

Temperature Optimum [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
-
 Acinetobacter baylyi

pH Range

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

General Information

General Information Comment Organism
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
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