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Literature summary for 6.2.1.B11 extracted from

  • Weiße, R.H.-J. ; Faust, A.; Schmidt, M.; Schönheit, P.; Scheidig, A.J.
    Structure of NDP-forming acetyl-CoA synthetase ACD1 reveals a large rearrangement for phosphoryl transfer (2016), Proc. Natl. Acad. Sci. USA, 113, E519-E528 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.2.1.B11

Crystallization (Commentary)

Crystallization (Comment) Organism
purified ckcACD1 enzyme in complex with phosphorylated His254alpha and in complex with ADP or with the nonhydrolyzable ATP analogue AMPPCP, X-ray diffraction structure determination and analysis at 1.9-2.4 A resolution Candidatus Korarchaeum cryptofilum

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Candidatus Korarchaeum cryptofilum
additional information the metal ion is coordinated by the side chain of Asp351alpha' Candidatus Korarchaeum cryptofilum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + acetate + CoA Candidatus Korarchaeum cryptofilum
-
 ADP + phosphate + acetyl-CoA
-
 r

Organism

Organism UniProt Comment Textmining
Candidatus Korarchaeum cryptofilum B1L3C9
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein phosphorylation of His254, conformation of the phosphorylated His is stabilized by ionic interaction with the side-chain carboxyl group of Glu213alpha, a hydrogen bridge provides an ideal geometry for the phosphorylation reaction by favoring the protonation state of the imidazole group. In addition, the phosphoryl moiety forms a hydrogen bond to the hydroxyl group of Ser160alpha. In the crystal structure ckcACD1-H, the phosphate moiety also interacts with a bound metal ion Candidatus Korarchaeum cryptofilum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + acetate + CoA
-
 Candidatus Korarchaeum cryptofilum ADP + phosphate + acetyl-CoA
-
 r
additional information to transmit an activated phosphoryl moiety from the acetyl-CoA binding site (within the alpha subunit) to the NDP-binding site (within the beta subunit), a distance of 51 A has to be bridged, binding mode of the Ac moiety within acetyl-CoA, and binding mode of Ado nucleotides within site II located in the beta subunit Candidatus Korarchaeum cryptofilum ?
-
 ?

Subunits

Subunits Comment Organism
heterotetramer unique arrangement of the ACD subunits alpha and beta within an alpha2beta2-heterotetrameric complex Candidatus Korarchaeum cryptofilum
More overall structure and domain arrangement of ckcACD1, overview Candidatus Korarchaeum cryptofilum

Synonyms

Synonyms Comment Organism
ACD
-
 Candidatus Korarchaeum cryptofilum
ckcACD1
-
 Candidatus Korarchaeum cryptofilum
NDP-forming acyl-CoA synthetase
-
 Candidatus Korarchaeum cryptofilum

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Candidatus Korarchaeum cryptofilum

General Information

General Information Comment Organism
evolution the ACD enzymes are considered to be primordial enzymes of ATP synthesis in the early evolution of life. The structure reveals a unique arrangement of the ACD subunits alpha and beta within an alpha2beta2-heterotetrameric complex. This arrangement significantly differs from other members of the superfamily. Residues Ser160alpha and Asp351alpha' are highly conserved throughout the ACD superfamily Candidatus Korarchaeum cryptofilum
physiological function the NDP-forming acyl-CoA synthetases (ACDs) catalyze the conversion of various CoA thioesters to the corresponding acids, conserving their chemical energy in form of ATP. The ACDs are the major energy-conserving enzymes in sugar and peptide fermentation of hyperthermophilic archaea Candidatus Korarchaeum cryptofilum