2.3.1.8: phosphate acetyltransferase
This is an abbreviated version!
For detailed information about phosphate acetyltransferase, go to the full flat file.
Word Map on EC 2.3.1.8
-
2.3.1.8
-
acetyl-coenzyme
-
methanosarcina
-
thermophila
-
formate-lyase
-
acetobutylicum
-
pta-ack
-
acetogenic
-
coash
-
acka-pta
-
2.7.2.1
-
phosphoketolase
-
acetoin
-
acetate-activating
-
butyryl-coa
-
tyrobutyricum
-
substrate-level
-
2,3-butanediol
-
acetate-grown
-
acetylphosphate
-
sulfoacetaldehyde
-
synthesis
-
biotechnology
-
biofuel production
- 2.3.1.8
-
acetyl-coenzyme
- methanosarcina
- thermophila
- formate-lyase
- acetobutylicum
-
pta-ack
-
acetogenic
- coash
-
acka-pta
-
2.7.2.1
- phosphoketolase
- acetoin
-
acetate-activating
- butyryl-coa
- tyrobutyricum
-
substrate-level
- 2,3-butanediol
-
acetate-grown
- acetylphosphate
- sulfoacetaldehyde
- synthesis
- biotechnology
- biofuel production
Reaction
Synonyms
acetyl-S-CoA: orthophosphate acetyltransferase, acetyltransferase, phosphate, aster yellows witches'-broom phosphotransacetylase-like enzyme, AYWB-PduL, EutD, Moth_0864, Moth_1181, pduL1, pduL2, PGN_1179, phosphate acetyltransferase, phosphoacylase, phosphotransacetylase, phosphotransacetylase EutD, phosphotransacetylase Pta, PTA, Pta-1, Pta-2, PtaII1, PtaII2
ECTree
Advanced search results
Activating Compound
Activating Compound on EC 2.3.1.8 - phosphate acetyltransferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
dithiothreitol
-
maxmimum activity in the presence of 1 mM dithiothreitol
PPIB
cytoplasmic cytophilin, interaction with phosphate acetyltransferase leads to enhanced activity and alteration in Km value. PPIase activity is not essential for these interactions, as PPIB F99A active site mutant still interacts with phosphate acetyltransferase, but PPIB activity is responsible for the observed phosphate acetyltransferase activity enhancement
-
additional information
-
not significant efects: NADH, ATP, phosphoenol pyruvate and aspartate, even at concentrations as high as 10 mM
-
NH4Cl
-
3fold stimulation at 40 mM. No significant increase in activity above 40 mM
pyruvate
-
isoform PtaII has 133% activity in the presence of 0.05 mM pyruvate
pyruvate
-
stimulates activity of wild-type enzyme 0.2fold over control, and the activity of the mutant enzyme R252H 3fold over control
pyruvate
-
stimulates wild-type activity, its effect is potentiated in the variants, being most pronounced on R252H