2.7.1.208: protein-Npi-phosphohistidine-maltose phosphotransferase
This is an abbreviated version!
For detailed information about protein-Npi-phosphohistidine-maltose phosphotransferase, go to the full flat file.
Word Map on EC 2.7.1.208
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2.7.1.208
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maltase
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glucose-induced
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maltose-inducible
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maltotriose
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mal-activator
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carlsbergensis
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baking
-
brewing
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nonfermenting
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bake
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leavening
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dough
-
alpha-glucoside
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alpha-methylglucoside
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glucose-repressed
- 2.7.1.208
- maltase
-
glucose-induced
-
maltose-inducible
- maltotriose
-
mal-activator
- carlsbergensis
-
baking
- brewing
-
nonfermenting
-
bake
-
leavening
-
dough
-
alpha-glucoside
- alpha-methylglucoside
-
glucose-repressed
Reaction
Synonyms
EC 2.7.1.69, EIICBAMal, EIImal, enzyme IIMal, MalP, MalT, maltose permease, maltose PTS, maltose PTS permease, maltose transporter, maltose-PTS transporter, maltose-specific permease, PtsG
ECTree
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Reference
Reference on EC 2.7.1.208 - protein-Npi-phosphohistidine-maltose phosphotransferase
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Webb, A.J.; Homer, K.A.; Hosie, A.H.
A phosphoenolpyruvate-dependent phosphotransferase system is the principal maltose transporter in Streptococcus mutans
J. Bacteriol.
189
3322-3327
2007
Streptococcus mutans, Streptococcus mutans UA159
Tangney, M.; Winters, G.; Mitchell, W.
Characterization of a maltose transport system in Clostridium acetobutylicum ATCC 824
J. Ind. Microbiol. Biotechnol.
27
298-306
2001
Clostridium acetobutylicum (Q93Q02), Clostridium acetobutylicum
Sauvageot, N.; Mokhtari, A.; Joyet, P.; Budin-Verneuil, A.; Blancato, V.S.; Repizo, G.D.; Henry, C.; Pikis, A.; Thompson, J.; Magni, C.; Hartke, A.; Deutscher, J.
Enterococcus faecalis uses a phosphotransferase system permease and a host colonization-related ABC transporter for maltodextrin uptake
J. Bacteriol.
199
e00878-16
2017
Enterococcus faecalis, Enterococcus faecalis JH2-2
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