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
General Information
General Information 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.
metabolism
-
anaerobic fermentative metabolism of glycerol. Proteome analysis as well as enzyme assays performed in cell-free extracts demonstrate that glycerol is degraded via glyceraldehyde-3-phosphate, which is further metabolized through the lower part of glycolysis leading to formation of mainly ethanol and hydrogen
physiological function
-
expression of phosphate acetyltransferase eutD restOres the ability of a strain lacking phosphate acetyltransferase pta and acetate kinase to grow on acetate as sole carbon source
physiological function
the substrate-binding site is located at the C-terminal PTA-PTB domain. The N-terminal P-loop NTPase domain is involved in expression of the maximal catalytic activity, stabilization of the hexameric native state, and phosphate acetyltransferase activity regulation by NADH, ATP, phosphoenolpyruvate, and pyruvate. The truncated protein Pta-F3 is able to complement the growth on acetate of an Escherichia coli mutant defective in acetyl-CoA synthetase and phosphate acetyltransferase activity
physiological function
the phosphotransacetylase Pta and acetate kinase Ack genes are tandemly located in the genome, and are cotranscribed as an operon. Inactivation of Pta or Ack by homologous recombination is successful only when the inactivated gene is expressed in trans
physiological function
-
the phosphotransacetylase Pta and acetate kinase Ack genes are tandemly located in the genome, and are cotranscribed as an operon. Inactivation of Pta or Ack by homologous recombination is successful only when the inactivated gene is expressed in trans
-