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Literature summary for 3.1.3.22 extracted from

  • Zeidler, S.; Hubloher, J.; Koenig, P.; Ngu, N.; Scholz, A.; Averhoff, B.; Mueller, V.
    Salt induction and activation of MtlD, the key enzyme in the synthesis of the compatible solute mannitol in Acinetobacter baumannii (2018), MicrobiologyOpen, 7, e00614 .
    View publication on PubMedView publication on EuropePMC
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Activating Compound

Activating Compound Comment Organism Structure
sodium glutamate highest stimulation up to 41 U/mg protein by sodium glutamate Acinetobacter baumannii

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Acinetobacter baumannii

Metals/Ions

Metals/Ions Comment Organism Structure
NaCl enzyme activity is strictly salt dependent. Highest stimulation is reached at 600 mM NaCl Acinetobacter baumannii

Organism

Organism UniProt Comment Textmining
Acinetobacter baumannii D0C7J2 bifunctional mannitol-1-phosphate dehydrogenase/phosphatase
-
Acinetobacter baumannii ATCC 19606 D0C7J2 bifunctional mannitol-1-phosphate dehydrogenase/phosphatase
-

Subunits

Subunits Comment Organism
? x * 82000, calculated from sequence Acinetobacter baumannii

Synonyms

Synonyms Comment Organism
HMPREF0010_00722
-
 Acinetobacter baumannii
MtlD
-
 Acinetobacter baumannii

Expression

Organism Comment Expression
Acinetobacter baumannii expression of mtlD is strongly dependent on high osmolarity, not discriminating between different salts or sugars. The presence of glycine betaine or choline represses promoter activation additional information

General Information

General Information Comment Organism
physiological function after deletion of the mtlD gene, cells no longer accumulate mannitol and growth is completely impaired at high salt concentrations Acinetobacter baumannii