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Literature summary for 2.3.1.B34 extracted from

  • Crosby, H.A.; Escalante-Semerena, J.C.
    The acetylation motif in AMP-forming Acyl coenzyme A synthases contains residues critical for acetylation and recognition by the protein acetyltransferase pat of Rhodopseudomonas palustris (2014), J. Bacteriol., 196, 1496-1504.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.B34

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetyl-CoA + [BtyA]-L-Lys Rhodopseudomonas palustris substrate is a AMP-forming acyl-CoA synthase, acetylation occurs at the catalytic lysine residue CoA + [BtyA]-N6-acetyl-L-Lys
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 ?
acetyl-CoA + [DcaA]-L-Lys Rhodopseudomonas palustris substrate is a AMP-forming acyl-CoA synthase, acetylation occurs at the catalytic lysine residue CoA + [DcaA]-N6-acetyl-L-Lys
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 ?
acetyl-CoA + [DcaB]-L-Lys Rhodopseudomonas palustris substrate is a AMP-forming acyl-CoA synthase, acetylation occurs at the catalytic lysine residue CoA + [DcaB]-N6-acetyl-L-Lys
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 ?
acetyl-CoA + [DcaC]-L-Lys Rhodopseudomonas palustris substrate is a AMP-forming acyl-CoA synthase, acetylation occurs at the catalytic lysine residue CoA + [DcaC]-N6-acetyl-L-Lys
-
 ?
acetyl-CoA + [LcsB mutant L500V]-L-Lys Rhodopseudomonas palustris wild-type AMP-forming acyl-CoA synthase LcsB is not a substrate, acetylation of mutant L500V occurs at the catalytic lysine residue CoA + [LcsB mutant L500V]-N6-acetyl-L-Lys
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 ?
acetyl-CoA + [PimA]-L-Lys534 Rhodopseudomonas palustris substrate is a AMP-forming acyl-CoA synthase CoA + [PimA]-N6-acetyl-L-Lys534 alanine substitutions at residues Pro528, Arg529, Thr530, Val532, and Gly533 of PimA result in variants that are acetylated less than 50% relative to the wild-type protein. C-terminal to the acetylation site, alanine substitutions at residues Arg537, Leu540, and Arg541 yield variants that also showed less than 50% of wild-type acetylation ?
acetyl-CoA + [VcsA]-L-Lys Rhodopseudomonas palustris substrate is a AMP-forming acyl-CoA synthase, acetylation occurs at the catalytic lysine residue CoA + [VcsA]-N6-acetyl-L-Lys
-
 ?
additional information Rhodopseudomonas palustris enzyme inactivates AMP-forming acyl-CoA synthases by acetylating the epsilon-amino group of a conserved, catalytic lysine residue. Substrate recognition motif is PK/RTXS/T/V/NGKX2K/R. The first residue, threonine, is located 4 amino acids upstream of the acetylation site. The second residue can be S/T/V/N and is located two positions upstream of the acetylation site. No substrate: long-chain acyl-CoA synthase B ?
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 ?

Organism

Organism UniProt Comment Textmining
Rhodopseudomonas palustris
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + [BtyA]-L-Lys substrate is a AMP-forming acyl-CoA synthase, acetylation occurs at the catalytic lysine residue Rhodopseudomonas palustris CoA + [BtyA]-N6-acetyl-L-Lys
-
 ?
acetyl-CoA + [DcaA]-L-Lys substrate is a AMP-forming acyl-CoA synthase, acetylation occurs at the catalytic lysine residue Rhodopseudomonas palustris CoA + [DcaA]-N6-acetyl-L-Lys
-
 ?
acetyl-CoA + [DcaB]-L-Lys substrate is a AMP-forming acyl-CoA synthase, acetylation occurs at the catalytic lysine residue Rhodopseudomonas palustris CoA + [DcaB]-N6-acetyl-L-Lys
-
 ?
acetyl-CoA + [DcaC]-L-Lys substrate is a AMP-forming acyl-CoA synthase, acetylation occurs at the catalytic lysine residue Rhodopseudomonas palustris CoA + [DcaC]-N6-acetyl-L-Lys
-
 ?
acetyl-CoA + [LcsB mutant L500V]-L-Lys wild-type AMP-forming acyl-CoA synthase LcsB is not a substrate, acetylation of mutant L500V occurs at the catalytic lysine residue Rhodopseudomonas palustris CoA + [LcsB mutant L500V]-N6-acetyl-L-Lys
-
 ?
acetyl-CoA + [PimA]-L-Lys534 substrate is a AMP-forming acyl-CoA synthase Rhodopseudomonas palustris CoA + [PimA]-N6-acetyl-L-Lys534 alanine substitutions at residues Pro528, Arg529, Thr530, Val532, and Gly533 of PimA result in variants that are acetylated less than 50% relative to the wild-type protein. C-terminal to the acetylation site, alanine substitutions at residues Arg537, Leu540, and Arg541 yield variants that also showed less than 50% of wild-type acetylation ?
acetyl-CoA + [VcsA]-L-Lys substrate is a AMP-forming acyl-CoA synthase, acetylation occurs at the catalytic lysine residue Rhodopseudomonas palustris CoA + [VcsA]-N6-acetyl-L-Lys
-
 ?
additional information enzyme inactivates AMP-forming acyl-CoA synthases by acetylating the epsilon-amino group of a conserved, catalytic lysine residue. Substrate recognition motif is PK/RTXS/T/V/NGKX2K/R. The first residue, threonine, is located 4 amino acids upstream of the acetylation site. The second residue can be S/T/V/N and is located two positions upstream of the acetylation site. No substrate: long-chain acyl-CoA synthase B Rhodopseudomonas palustris ?
-
 ?

Synonyms

Synonyms Comment Organism
Pat
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 Rhodopseudomonas palustris
protein acetyltransferase
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 Rhodopseudomonas palustris