Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
-
ATP, ADP and AMP do not affect the activity of AfM1PDH, suggesting the absence of flux control by cellular energy charge at the level of D-fructose 6-phosphate reduction
evolution
-
the enzyme belongs to the medium chain dehydrogenases
evolution
sequence analysis suggests that algal and apicomplexa M1PDHs represent a distinct type of mannitol-1-phosphate dehydrogenase in the PSLDR family
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
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
-
malfunction
-
deletion of gene mtlD results in a complete loss of salt-dependent mannitol biosynthesis
malfunction
the Corynebacterium glutamicum arabitol-negative DELTAmtlD deletion mutant can be complemented by heterologous expression of Bacillus methanolicus strain MGA3 operon atlABCD or gene atlD
metabolism
-
the enzyme is involved in the mannitol cycle in the fungus
metabolism
-
mannitol-1-phosphate dehydrogenase mediates the first step of two-step pathway for osmo-induced synthesis of mannitol, regulated by salinity on the transcriptional as well as on the activity level, overview
metabolism
the enzyme catalyzes the first step of the synthesis of mannitol, i.e. reduction of the photo-assimilate fructose-6-phosphate, mannitol cycle, overview
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
metabolism
the enzyme is involved in the arabitol catabolism and the pentose phosphate pathway, model of the pathways for arabitol catabolism in bacteria, overview
metabolism
-
the enzyme catalyzes the first step of the synthesis of mannitol, i.e. reduction of the photo-assimilate fructose-6-phosphate, mannitol cycle, overview
-
metabolism
-
the enzyme is involved in the arabitol catabolism and the pentose phosphate pathway, model of the pathways for arabitol catabolism in bacteria, overview
-
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
-
metabolism
-
the enzyme is involved in the arabitol catabolism and the pentose phosphate pathway, model of the pathways for arabitol catabolism in bacteria, overview
-
physiological function
crucial role of BbMPD in the mannitol biosynthesis of Beauveria bassiana
physiological function
-
formation of mannitol is an essential component of the temperature stress response of Aspergillus fumigatus. Enhanced biosynthesis of d-mannitol via AfM1PDH-catalyzed conversion of fructose 6-phosphate might contribute extra robustness to Aspergillus fumigatus under high temperature conditions
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
physiological function
after deletion of the mtlD gene, cells no longer accumulate mannitol and growth is completely impaired at high salt concentrations
physiological function
Corynebacterium glutamicum is a natural D-arabitol utilizer that requires arabitol-utilizing mannitol-1-phosphate 5-dehydrogenase MtlD for arabitol catabolism
physiological function
M1PDH is essential to endure pH, high salt concentration, and oxidative stress and is required for preventing osmotic burst by regulating pressure potential imposed by mannitol. In a mouse infection model, M1PDH is essential for bacterial survival during infection
physiological function
MpdA deletion leads to ascosporogenesis failure and results in small cleistothecia with no functional ascospores. MpdA modulates the expression of key development- and meiosis-regulatory genes during sexual development. The MpdA deletion increases hyphal branching and decreases conidial heat resistance. Mannitol production in conidia shows no difference, whereas it is decreased in mycelia and sexual cultures
physiological function
when the mannitol-1-phosphate 5-dehydrogenase gene MtlD is targeted by CRISPRi, mtlD RNA levels, and MtlD specific activities in crude extracts are decreased to about 50 %, which results in reduced biomass formation from mannitol
physiological function
-
MpdA deletion leads to ascosporogenesis failure and results in small cleistothecia with no functional ascospores. MpdA modulates the expression of key development- and meiosis-regulatory genes during sexual development. The MpdA deletion increases hyphal branching and decreases conidial heat resistance. Mannitol production in conidia shows no difference, whereas it is decreased in mycelia and sexual cultures
-
physiological function
-
M1PDH is essential to endure pH, high salt concentration, and oxidative stress and is required for preventing osmotic burst by regulating pressure potential imposed by mannitol. In a mouse infection model, M1PDH is essential for bacterial survival during infection
-
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
-
physiological function
-
after deletion of the mtlD gene, cells no longer accumulate mannitol and growth is completely impaired at high salt concentrations
-
physiological function
-
when the mannitol-1-phosphate 5-dehydrogenase gene MtlD is targeted by CRISPRi, mtlD RNA levels, and MtlD specific activities in crude extracts are decreased to about 50 %, which results in reduced biomass formation from mannitol
-