4.1.2.22: fructose-6-phosphate phosphoketolase
This is an abbreviated version!
For detailed information about fructose-6-phosphate phosphoketolase, go to the full flat file.
Word Map on EC 4.1.2.22
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4.1.2.22
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bifidobacteria
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hsp60
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faeces
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longum
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breve
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dna-dna
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biotechnology
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non-spore-forming
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bumblebee
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catalase-negative
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heterofermentative
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adolescentis
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gram-positive-staining
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mupirocin
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bifidobacteriaceae
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dentium
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asporogenous
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saguinus
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globosum
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animalis
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tamarin
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pcr-dgge
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analysis
- 4.1.2.22
-
bifidobacteria
- hsp60
-
faeces
- longum
- breve
-
dna-dna
- biotechnology
-
non-spore-forming
-
bumblebee
-
catalase-negative
-
heterofermentative
- adolescentis
-
gram-positive-staining
- mupirocin
- bifidobacteriaceae
- dentium
-
asporogenous
-
saguinus
- globosum
- animalis
- tamarin
-
pcr-dgge
- analysis
Reaction
Synonyms
All1483, All2567, F-6-ppk, F6P phosphoketolase, F6PPK, Fructose-6-phosphate phosphoketolase, Phosphoketolase, fructose 6-phosphate, X5P/F6P phosphoketolase, X5P/F6P PK, Xf2, Xfp, XFPK, Xpf, xylulose 5-phosphate/fructose 6-phosphate phosphoketolase, xylulose-5-phosphate/fructose-6-phosphate phosphoketolase
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Inhibitors
Inhibitors on EC 4.1.2.22 - fructose-6-phosphate phosphoketolase
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ATP
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phosphoenolpyruvate and oxaloacetic acid share the same or have overlapping allosteric binding sites, while ATP binds at a separate site
additional information
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the enzyme is unaffected by the presence of ATP, AMP, pyruvate, and acetate
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phosphoenolpyruvate and oxaloacetic acid share the same or have overlapping allosteric binding sites, while ATP binds at a separate site. AMP and phosphoenolpyruvate/oxaloacetic acid operate independently, with AMP activating Xfp2 and phosphoenolpyruvate/oxaloacetic acid inhibiting the activated enzyme
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phosphoenolpyruvate and oxaloacetic acid share the same or have overlapping allosteric binding sites, while ATP binds at a separate site. AMP and phosphoenolpyruvate/oxaloacetic acid operate independently, with AMP activating Xfp2 and phosphoenolpyruvate/oxaloacetic acid inhibiting the activated enzyme