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Literature summary for 6.2.1.2 extracted from

  • Meng, Y.; Ingram-Smith, C.; Cooper, L.L.; Smith, K.S.
    Characterization of an archaeal medium-chain acyl coenzyme A synthetase from Methanosarcina acetivorans (2010), J. Bacteriol., 192, 5982-5990.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.2.1.2

Cloned(Commentary)

Cloned (Comment) Organism
heterologous production in Escherichia coli Methanosarcina acetivorans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.09
-
 CoA pH 7.5, 55°C Methanosarcina acetivorans
4.21
-
 ATP pH 7.5, 55°C Methanosarcina acetivorans
8.92
-
 2-methylbutyrate pH 7.5, 55°C Methanosarcina acetivorans

Organism

Organism UniProt Comment Textmining
Methanosarcina acetivorans Q8TLW1
-
-
Methanosarcina acetivorans DSM 2834 Q8TLW1
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Methanosarcina acetivorans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 2-methylbutyrate + CoA when propionate or other less favorable acyl substrates, such as butyrate, 2-methylpropionate, or 2-methylvalerate, are utilized, the acyl-CoA is not produced or is produced at reduced levels. Instead, acyl-AMP and diphosphate are released in the absence of CoA, whereas in the presence of CoA, the intermediate is broken down into AMP and the acyl substrate, which are released along with diphosphate. These results suggest that although acyl-CoA synthetases may have the ability to utilize a broad range of substrates for the acyl-adenylate-forming first step of the reaction, the intermediate may not be suitable for the thioester-forming second step Methanosarcina acetivorans AMP + diphosphate + 2-methylbutyryl-CoA
-
 ?
ATP + 2-methylbutyrate + CoA when propionate or other less favorable acyl substrates, such as butyrate, 2-methylpropionate, or 2-methylvalerate, are utilized, the acyl-CoA is not produced or is produced at reduced levels. Instead, acyl-AMP and diphosphate are released in the absence of CoA, whereas in the presence of CoA, the intermediate is broken down into AMP and the acyl substrate, which are released along with diphosphate. These results suggest that although acyl-CoA synthetases may have the ability to utilize a broad range of substrates for the acyl-adenylate-forming first step of the reaction, the intermediate may not be suitable for the thioester-forming second step Methanosarcina acetivorans DSM 2834 AMP + diphosphate + 2-methylbutyryl-CoA
-
 ?

Synonyms

Synonyms Comment Organism
Macs
-
 Methanosarcina acetivorans
medium-chain acyl coenzyme A synthetase
-
 Methanosarcina acetivorans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
55
-
 assay at Methanosarcina acetivorans

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.58
-
 2-methylbutyrate pH 7.5, 55°C Methanosarcina acetivorans
1.94
-
 ATP pH 7.5, 55°C Methanosarcina acetivorans
2.15
-
 CoA pH 7.5, 55°C Methanosarcina acetivorans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Methanosarcina acetivorans

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.18
-
 2-methylbutyrate pH 7.5, 55°C Methanosarcina acetivorans
0.46
-
 ATP pH 7.5, 55°C Methanosarcina acetivorans
0.53
-
 CoA pH 7.5, 55°C Methanosarcina acetivorans