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Literature summary for 6.2.2.2 extracted from

  • Ge, Y.; Czekster, C.M.; Miller, O.K.; Botting, C.H.; Schwarz-Linek, U.; Naismith, J.H.
    Insights into the mechanism of the cyanobactin heterocyclase enzyme (2019), Biochemistry, 58, 2125-2132 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.2.2.2

Organism

Organism UniProt Comment Textmining
Microcystis aeruginosa A8Y998
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Microcystis aeruginosa NIES-298 A8Y998
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + [PatE2K]-(L-amino acyl-L-cysteine)
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 Microcystis aeruginosa ADP + phosphate + [PatE2K]-(1S,4R)-2-(C-substituted-aminomethyl)-4-acyl-2-thiazoline
-
 ?
ATP + [PatE2K]-(L-amino acyl-L-cysteine)
-
 Microcystis aeruginosa NIES-298 ADP + phosphate + [PatE2K]-(1S,4R)-2-(C-substituted-aminomethyl)-4-acyl-2-thiazoline
-
 ?
ATP + [PatE2K]-(L-amino acyl-L-threonine)
-
 Microcystis aeruginosa ADP + phosphate + [PatE2K]-(S,S)-2-(C-substituted-aminomethyl)-4-acyl-5-methyl-2-oxazoline
-
 ?
ATP + [TruE2]-(L-amino acyl-L-cysteine)
-
 Microcystis aeruginosa ADP + phosphate + [TruE2]-(1S,4R)-2-(C-substituted-aminomethyl)-4-acyl-2-thiazoline
-
 ?
ATP + [TruE2]-(L-amino acyl-L-cysteine)
-
 Microcystis aeruginosa NIES-298 ADP + phosphate + [TruE2]-(1S,4R)-2-(C-substituted-aminomethyl)-4-acyl-2-thiazoline
-
 ?
ATP + [TruE2]-(L-amino acyl-L-threonine)
-
 Microcystis aeruginosa ADP + phosphate + [TruE2]-(S,S)-2-(C-substituted-aminomethyl)-4-acyl-5-methyl-2-oxazoline
-
 ?
ATP + [TruE2]-(L-amino acyl-L-threonine)
-
 Microcystis aeruginosa NIES-298 ADP + phosphate + [TruE2]-(S,S)-2-(C-substituted-aminomethyl)-4-acyl-5-methyl-2-oxazoline
-
 ?
additional information in the absence of peptide substrate, MicD is likely catalyzing solely ATP hydrolysis to ADP and then to AMP, while in the presence of substrate, ATP consumption is coupled to heterocyclization. Presence of ATP is required for catalysis. ATP analogue AMP-CPP supports catalysis, while AMP-PCP does not Microcystis aeruginosa ?
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additional information the order of reaction for threonines is different from that of cysteines and depends in part on a leader peptide within the substrate Microcystis aeruginosa ?
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additional information in the absence of peptide substrate, MicD is likely catalyzing solely ATP hydrolysis to ADP and then to AMP, while in the presence of substrate, ATP consumption is coupled to heterocyclization. Presence of ATP is required for catalysis. ATP analogue AMP-CPP supports catalysis, while AMP-PCP does not Microcystis aeruginosa NIES-298 ?
-
-
additional information the order of reaction for threonines is different from that of cysteines and depends in part on a leader peptide within the substrate Microcystis aeruginosa NIES-298 ?
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-

Synonyms

Synonyms Comment Organism
adenylation/heterocyclization protein
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 Microcystis aeruginosa
MCAD
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 Microcystis aeruginosa
micD
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 Microcystis aeruginosa

General Information

General Information Comment Organism
physiological function reaction mechanism, the gamma-phosphate of ATP is transferred in a kinase mechanism to the substrate to yield a phosphorylated intermediate common to all YcaO domain proteins. In cyanobactin heterocyclases, this phosphorylated intermediate, in a proportion of turnovers, reacts with ADP to yield AMP and diphosphate Microcystis aeruginosa
physiological function in a kinase mechanism, the gamma-phosphate of ATP is transferred to the substrate to yield a phosphorylated intermediate common to all YcaO domains. In cyanobactin heterocyclases, this phosphorylated intermediate, in a proportion of turnovers, reacts with ADP to yield AMP and diphosphate Microcystis aeruginosa