1.97.1.4: [formate-C-acetyltransferase]-activating enzyme
This is an abbreviated version!
For detailed information about [formate-C-acetyltransferase]-activating enzyme, go to the full flat file.
Word Map on EC 1.97.1.4
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1.97.1.4
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glycyl
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5\'-deoxyadenosyl
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iron-sulfur
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organometallic
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adomet
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oxygen-sensitive
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homolytic
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endor
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adenosylmethionine
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5'-deoxyadenosine
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h-atom
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sulfonium
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knappe
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deoxyadenosyl
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medicine
- 1.97.1.4
-
glycyl
-
5\'-deoxyadenosyl
-
iron-sulfur
-
organometallic
- adomet
-
oxygen-sensitive
-
homolytic
-
endor
- adenosylmethionine
- 5'-deoxyadenosine
-
h-atom
-
sulfonium
-
knappe
-
deoxyadenosyl
- medicine
Reaction
Synonyms
Activase, pyruvate formate-lyase, Formate acetyltransferase activase, Formate-lyase-activating enzyme, PFL, PFL activase, PFL activating enzyme, PFL-activating enzyme, PFL-AE, PFL-glycine:S-adenosyl-L-methionine H transferase (flavodoxin-oxidizing, S-adenosyl-L-methionine-cleaving), PflA, pyruvate formate lyase activating enzyme, Pyruvate formate-lyase activase, Pyruvate formate-lyase activating enzyme, pyruvate formate-lyase-activating enzyme
ECTree
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Engineering
Engineering on EC 1.97.1.4 - [formate-C-acetyltransferase]-activating enzyme
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C102S
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mutant enzymes C12S, C94S, C102S display full holoactivase activity, albeit absolute values are slightly lower, by a factor of 2 than the value of the wild type enzyme. Mutant enzymes C29S, C33S and C36S are catalytically incompetent
C12S
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mutant enzymes C12S, C94S, C102S display full holoactivase activity, albeit absolute values are slightly lower, by a factor of 2 than the value of the wild type enzyme. Mutant enzymes C29S, C33S and C36S are catalytically incompetent
C29S
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mutant enzymes C12S, C94S, C102S display full holoactivase activity, albeit absolute values are slightly lower, by a factor of 2 than the value of the wild type enzyme. Mutant enzymes C29S, C33S and C36S are catalytically incompetent
C33S
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mutant enzymes C12S, C94S, C102S display full holoactivase activity, albeit absolute values are slightly lower, by a factor of 2 than the value of the wild type enzyme. Mutant enzymes C29S, C33S and C36S are catalytically incompetent
C36S
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mutant enzymes C12S, C94S, C102S display full holoactivase activity, albeit absolute values are slightly lower, by a factor of 2 than the value of the wild type enzyme. Mutant enzymes C29S, C33S and C36S are catalytically incompetent
C94S
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mutant enzymes C12S, C94S, C102S display full holoactivase activity, albeit absolute values are slightly lower, by a factor of 2 than the value of the wild type enzyme. Mutant enzymes C29S, C33S and C36S are catalytically incompetent
D104A
site-directed mutagenesis, mutation of the cation binding site, the D104A variant has very low activity in presence of KCl compared to the wild-type, S-adenosyl-L-methionine does not bind well in this variant
D129A
site-directed mutagenesis, mutation of the cation binding site, the mutant retains the ability to bind cations, the variant binds M+ and SAM in a manner similar to wild-type
additional information
for activity assay, the enzyme PFL-AE is attached to a CM5 sensor chip using standard thiol coupling procedures
additional information
recombinant coexpression of the enzyme with pyruvate format lyase and flavodoxin or ferredoxin in Saccharomyces cerevisiae leads to over 20fold increased expression of endogenous formate dehydrogenases FDH1 and FDH2