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

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

[formate C-acetyltransferase]-glycin-2-yl radical

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

1 Oxidoreductases

1.97 Other oxidoreductases

1.97.1 Sole sub-subclass for oxidoreductases that do not belong in the other subclasses

1.97.1.4 [formate-C-acetyltransferase]-activating enzyme

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Results	in table
3	Activating Compound
11817	AA Sequence
1	Application
1	CAS Registry Number
9	Cloned(Commentary)
8	Cofactor
1	Crystallization (Commentary)
1	Expression
10	General Information
4	Inhibitors
3	KM Value [mM]
3	Localization
14	Metals/Ions
8	Molecular Weight [Da]
5	Natural Substrates/ Products (Substrates)
27	Organism
2	PDB ID
4	pH Optimum
1	pI Value
10	Protein Variants
5	Purification (Commentary)
4	Reaction
2	Reaction Type
26	Reference
1	Source Tissue
3	Specific Activity [micromol/min/mg]
1	Storage Stability
29	Substrates and Products (Substrate)
5	Subunits
27	Synonyms
1	Systematic Name
3	Temperature Optimum [°C]

Metals Ions

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Metals Ions on EC 1.97.1.4 - [formate-C-acetyltransferase]-activating enzyme

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Cobalt

Escherichia coli

Co(II) and Cu(II) can be reconstituted into the protein with similar stoichiometry

14934

copper

Escherichia coli

Co(II) and Cu(II) can be reconstituted into the protein with similar stoichiometry

Fe2+

Iron

K+

the presence and identity of the bound monovalent cation, requiring a K+ ion bound in the active site for optimal activity

745175

Na+

Escherichia coli

P0A9N4

Na+ as the most likely ion present in the solved enzyme structures, and pulsed electron nuclear double resonance (ENDOR) demonstrates that the same cation site is occupied by 23Na in the solution state of the as isolated enzyme

745175

[4Fe-4S] cluster

2 entries

additional information

Escherichia coli

P0A9N4

enzyme PFL-AE binds a catalytically essential monovalent cation at its active site. PFL-AE is thus a type I M+-activated enzyme whose M+ controls reactivity by interactions with the cosubstrate, SAM, which is bound to the catalytic iron-sulfur cluster. PFL-AE in the absence of any simple monovalent cations has little or no activity, and among monocations, going down Group 1 of the periodic table from Li+ to Cs+, PFL-AE activity sharply maximizes at K+ and NH4+. Cation binding site structure, e.g. with Mg2+, Cs+, Ca2+, Tl+, Li+, Zn2+, K+, NH4+, and Na+, overview. Modeling of different cations bound to the cation binding site of the enzyme, negative Fo-Fc electron density appears when the site is modeled as potassium or calcium, more extensive positive Fo-Fc electron density is present in the site when modeled with water than when modeled with sodium or magnesium. Residue D104 is important for cation binding

745175