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
2.3.1.8 phosphate acetyltransferaseAdvanced search results
results (
results (Engineering
Engineering 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.
top
PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D316E
kcat for the reaction of acetyl phosphate and CoA is 2.4fold lower than wild-type value, Km for CoA is 1.1fold higher than wild-type value, Km for acetyl phosphate is 1.4fold lower than wild-type value
R133Q
R310A
kcat for the reaction of acetyl phosphate and CoA is 22.6fold lower than wild-type value, Km for CoA is 1.8fold higher than wild-type value, Km for acetyl phosphate is 122fold higher than wild-type value
R310K
kcat for the reaction of acetyl phosphate and CoA is 472fold lower than wild-type value, Km for CoA is 1.8fold higher than wild-type value, Km for acetyl phosphate is 2.9fold higher than wild-type value
R310Q
R87Q
S309A
kcat for the reaction of acetyl phosphate and CoA is 358fold lower than wild-type value, Km for CoA is nearly identical to wild-type value, Km for acetyl phosphate is 1.96fold lower than wild-type value
S309C
kcat for the reaction of acetyl phosphate and CoA is 851fold lower than wild-type value, Km for CoA is1.4 fold higher than wild-type value, Km for acetyl phosphate is 1.4fold higher than wild-type value
S309T
kcat for the reaction of acetyl phosphate and CoA is 337fold lower than wild-type value, Km for CoA is 1.8fold lower than wild-type value, Km for acetyl phosphate is nearly identical to wild-type value
G300A
-
the mutant of isoform PtaII shows reduced activity compared to the wild type enzyme
G300D
-
the mutant of isoform PtaII shows reduced activity compared to the wild type enzyme
D309A
complete loss of activity, mutation does not affect the dimerization
D318A
complete loss of activity, mutant displays a broad biphasic pattern in gel filtration
R135A
21% decrease in specific activity, mutation does not affect the dimerization
R312A
complete loss of activity, mutation does not affect the dimerization
R89A
58% decrease in specific activity, mutation does not affect the dimerization
S311A
complete loss of activity, mutation does not affect the dimerization
D318A
-
complete loss of activity, mutant displays a broad biphasic pattern in gel filtration
-
R135A
-
21% decrease in specific activity, mutation does not affect the dimerization
-
R312A
-
complete loss of activity, mutation does not affect the dimerization
-
R89A
-
58% decrease in specific activity, mutation does not affect the dimerization
-
S311A
-
complete loss of activity, mutation does not affect the dimerization
-
G273D
M294I
R252H
additional information
R310Q
kcat for the reaction of acetyl phosphate and CoA is 75.2fold lower than wild-type value, Km for CoA is 2.8fold higher than wild-type value, Km for acetyl phosphate is 4.2fold higher than wild-type value
G273D
-
kcat for reaction with acetyl-CoA and phosphate is 3fold higher than wild-type value, kcat for reaction with CoA and acetyl phosphate is 2.3fold higher than wild-type value. Mutant enzyme shows less aggregation than wild type enzyme
G273D
-
kcat/Km for CoA is 2.2fold higher than wild-type value. kcat/KM for acetoacetyl-CoA is 3.6fold higher than wild-type value. Lower proportion of large enzyme aggregates compared with wild-type enzyme
M294I
-
kcat for reaction with acetyl-CoA and phosphate is 143fold lower than wild-type value, kcat for reaction with CoA and acetyl phosphate is 1.4fold lower than wild-type value. Mutant enzyme shows less aggregation than wild type enzyme
M294I
-
kcat/Km for CoA is 1.7fold higher than wild-type value. kcat/KM for acetoacetyl-CoA is 1.2lower higher than wild-type value. Lower proportion of large enzyme aggregates compared with wild-type enzyme
R252H
-
kcat for reaction with acetyl-CoA and phosphate is 2.5fold higher than wild-type value, kcat for reaction with CoA and acetyl phosphate is 2.5fold higher than wild-type value. No inhibition by NADH. Mutant enzyme shows less aggregation than wild type enzyme
R252H
-
kcat/Km for CoA is 2.6fold higher than wild-type value. kcat/KM for acetoacetyl-CoA is 1.6fold higher than wild-type value. Lower proportion of large enzyme aggregates compared with wild-type enzyme
additional information
construction of truncated mutants Pta-F1, consisting of the PTA-PTB domains, mutant Pta-F2, consisting of the PTA-PTB domains plus part of the DRTGG motif, and Pta-F3, consisting of the PTA-PTB domains plus the complete DRTGG motif. CD spectra for Pta-F1, Pta-F2 and Pta-F3 are comparable, but not identical, to the spectrum of the entire protein
additional information
-
construction of truncated mutants Pta-F1, consisting of the PTA-PTB domains, mutant Pta-F2, consisting of the PTA-PTB domains plus part of the DRTGG motif, and Pta-F3, consisting of the PTA-PTB domains plus the complete DRTGG motif. CD spectra for Pta-F1, Pta-F2 and Pta-F3 are comparable, but not identical, to the spectrum of the entire protein
