7.5.2.1: ABC-type maltose transporter
This is an abbreviated version!
For detailed information about ABC-type maltose transporter, go to the full flat file.
Word Map on EC 7.5.2.1
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7.5.2.1
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maltose-binding
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maltodextrins
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outward-facing
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proteoliposomes
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maltotriose
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nanodiscs
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atp-bound
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inward-facing
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atp-binding-cassette
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lager
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q-loops
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eiiaglc
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analysis
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synthesis
- 7.5.2.1
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maltose-binding
- maltodextrins
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outward-facing
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proteoliposomes
- maltotriose
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nanodiscs
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atp-bound
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inward-facing
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atp-binding-cassette
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lager
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q-loops
- eiiaglc
- analysis
- synthesis
Reaction
Synonyms
ATP phosphohydrolase (maltose-importing), Cg2463, EC 3.6.3.19, GlvC, Mal-EFGK2, Mal11, MalE, MalE-FGK2, MalF, MalFGK2, MalFGK2-E, MalG511, MalK, MalK2, malK3, MalP, MalT, MALT2, MALT4, maltose ABC transporter, maltose ABC transporter MALFGK2-E, maltose ABC-type transporter, maltose ATP binding cassette transporter, maltose ATP-binding cassette importer, maltose ATP-binding cassette transporter, maltose importer, maltose transporter, maltose transporter ATPase, maltose transporter MalFGK2, maltose-specific enzyme IICB, maltose-transporting ATPase, maltose/maltodextrin ABC transporter, More, MuSK, proton-maltose symporter
ECTree
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General Information
General Information on EC 7.5.2.1 - ABC-type maltose transporter
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malfunction
metabolism
physiological function
additional information
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a series of spontaneous mutants of Lactococcus lactis IL1403 show average 6 to 11fold lowered sensitivities to the circular bacteriocin garvicin ML and also changes in carbohydrate metabolism, specifically loss of the ability to metabolize starch and maltose, overview. Complementation of the mutants with genes malEFG recovers normal sensitivity to the bacteriocin
malfunction
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the addition of ATP and EDTA (to trigger the outwardfacing conformation) to the MBP-MalFGK2 system in the absence of maltose increases the mobility of W62C-SL in the MalG-DELTAscoop system but decreases it in the wild-type
malfunction
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a series of spontaneous mutants of Lactococcus lactis IL1403 show average 6 to 11fold lowered sensitivities to the circular bacteriocin garvicin ML and also changes in carbohydrate metabolism, specifically loss of the ability to metabolize starch and maltose, overview. Complementation of the mutants with genes malEFG recovers normal sensitivity to the bacteriocin
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the type I maltose ABC importer is encoded within the maltose regulon, which enables the bacteria to feed on maltose and maltodextrins, alpha-1,4-linked oligosaccharides up to seven glucose units, formed by enzymatic cleavage of starch or glycogen
metabolism
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the type I maltose ABC importer is encoded within the maltose regulon, which enables the bacteria to feed on maltose and maltodextrins, alpha-1,4-linked oligosaccharides up to seven glucose units, formed by enzymatic cleavage of starch or glycogen. The C-terminal domain of MalK has a dual regulatory function: it controls the activity of MalT, the positive transcriptional regulator of the maltose regulon, and it is the primary site at which dephosphorylated enzyme IIAGlc of the phosphoenolpyruvate phosphotransferase system binds, preventing maltose uptake
metabolism
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the maltose ABC transporter is carbon catabolite repression-regulated
metabolism
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the maltose transporter MalFGK2, together with the substrate-binding protein MalE, is a ABC transporter. MalE is bound in the periplasm with high-affinity to MalFGK2 to facilitate the acquisition of maltose. When the maltose concentration exceeds the transport capacity, MalE captures maltose and dissociates from the transporte, from the transporter past a threshold maltose concentration, in vivo, mechanism, overview. Maltose is both substrate and regulator of its own transporter, i.e. a homotropic regulator
metabolism
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the maltose ABC transporter is carbon catabolite repression-regulated
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essential role of the maltose ABC transporter in the antimicrobial activity of garvicin ML
physiological function
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the ATPase activity of the maltose transporter MalFGK2 is dependent on interactions with the maltose-binding protein, MBP
physiological function
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the enzyme couples the energy from ATP hydrolysis to the active transport of substrates across the membrane
physiological function
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the maltose ABC transporter MalFGK2 converts chemical energy from ATP hydrolysis to mechanical work for maltose substrate translocation. A periplasmic maltose-binding protein, MBP, is required to stimulate the ATPase activity of the transporter
physiological function
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the enzyme genes MALT2 and MALT4 are essential for growth on maltose
physiological function
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essential role of the maltose ABC transporter in the antimicrobial activity of garvicin ML
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physiological function
Saccharomyces eubayanus CBS 12357T
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the enzyme genes MALT2 and MALT4 are essential for growth on maltose
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a malEFG-a deletion mutant is unable to grow in a minimal medium with maltose as sole carbon source and produce avermectin. Maltose utilization and avermectin production are restored by introduction of a single copy of malEFG-a. Overexpression of malEFG-a improves the utilization rate of starch, and thereby enhances avermectin production
additional information
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in the absence of MBP, MalFGK2 forms an inwardfacing conformation with the transmembrane-maltose-binding site exposed to the cytoplasm
additional information
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a malEFG-a deletion mutant is unable to grow in a minimal medium with maltose as sole carbon source and produce avermectin. Maltose utilization and avermectin production are restored by introduction of a single copy of malEFG-a. Overexpression of malEFG-a improves the utilization rate of starch, and thereby enhances avermectin production
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