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Literature summary extracted from

  • Musfeldt, M.; Schonheit, P.
    Novel type of ADP-forming acetyl coenzyme A synthetase in hyperthermophilic archaea: heterologous expression and characterization of isoenzymes from the sulfate reducer Archaeoglobus fulgidus and the methanogen Methanococcus jannaschii (2002), J. Bacteriol., 184, 636-644.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.2.1.B11 overexpressed in Escherichia coli Archaeoglobus fulgidus
6.2.1.B11 overexpressed in Escherichia coli Methanocaldococcus jannaschii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.2.1.B11 0.007
-
 ADP pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 0.01
-
 acetyl-CoA pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 0.015
-
 ADP pH 8.0, 55°C Methanocaldococcus jannaschii
6.2.1.B11 0.017
-
 phenylacetyl-CoA pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 0.025
-
 CoA pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 0.03
-
 ATP pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 0.037
-
 acetyl-CoA pH 8.0, 55°C Methanocaldococcus jannaschii
6.2.1.B11 0.11
-
 phosphate pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 0.11
-
 phenylacetate pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 0.13
-
 ATP pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 0.34
-
 acetate pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 0.47
-
 phosphate pH 8.0, 55°C Methanocaldococcus jannaschii
6.2.1.B11 0.53
-
 CoA pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 1.24
-
 indole-3-acetate pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 2.5
-
 phenylacetate pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 2.58
-
 acetate pH 8.0, 55°C Archaeoglobus fulgidus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.2.1.B11 Ca2+ enzyme activity requires divalent cations. Mg2+(100%), which is the most effective, can be partially replaced by Co2+ (51%), Mn2+ (38%), and to a lesser extent (less than 20%) by Fe2+, Zn2+, Ni2+, Ca2+, and Cu2+ Archaeoglobus fulgidus
6.2.1.B11 Co2+ enzyme activity requires divalent cations. Mg2+(100%), which is the most effective, can be partially replaced by Co2+ (51%), Mn2+ (38%), and to a lesser extent (less than 20%) by Fe2+, Zn2+, Ni2+, Ca2+, and Cu2+ Archaeoglobus fulgidus
6.2.1.B11 Cu2+ activity depends on divalent cations. Mg2+which is most effective, could partially be replaced by Mn2+, Zn2+, and Cu2+ (each 30 to 40%) Archaeoglobus fulgidus
6.2.1.B11 Cu2+ enzyme activity requires divalent cations. Mg2+(100%), which is the most effective, can be partially replaced by Co2+ (51%), Mn2+ (38%), and to a lesser extent (less than 20%) by Fe2+, Zn2+, Ni2+, Ca2+, and Cu2+ Archaeoglobus fulgidus
6.2.1.B11 Fe2+ enzyme activity requires divalent cations. Mg2+(100%), which is the most effective, can be partially replaced by Co2+ (51%), Mn2+ (38%), and to a lesser extent (less than 20%) by Fe2+, Zn2+, Ni2+, Ca2+, and Cu2+ Archaeoglobus fulgidus
6.2.1.B11 Mg2+ activity depends on divalent cations. Mg2+which is most effective, could partially be replaced by Mn2+, Zn2+, and Cu2+ (each 30 to 40%) Archaeoglobus fulgidus
6.2.1.B11 Mg2+ enzyme activity requires divalent cations. Mg2+(100%), which is the most effective, can be partially replaced by Co2+ (51%), Mn2+ (38%), and to a lesser extent (less than 20%) by Fe2+, Zn2+, Ni2+, Ca2+, and Cu2+ Archaeoglobus fulgidus
6.2.1.B11 Mn2+ activity depends on divalent cations. Mg2+which is most effective, could partially be replaced by Mn2+, Zn2+, and Cu2+ (each 30 to 40%) Archaeoglobus fulgidus
6.2.1.B11 Mn2+ enzyme activity requires divalent cations. Mg2+(100%), which is the most effective, can be partially replaced by Co2+ (51%), Mn2+ (38%), and to a lesser extent (less than 20%) by Fe2+, Zn2+, Ni2+, Ca2+, and Cu2+ Archaeoglobus fulgidus
6.2.1.B11 Ni2+ enzyme activity requires divalent cations. Mg2+(100%), which is the most effective, can be partially replaced by Co2+ (51%), Mn2+ (38%), and to a lesser extent (less than 20%) by Fe2+, Zn2+, Ni2+, Ca2+, and Cu2+ Archaeoglobus fulgidus
6.2.1.B11 Zn2+ activity depends on divalent cations. Mg2+which is most effective, could partially be replaced by Mn2+, Zn2+, and Cu2+ (each 30 to 40%) Archaeoglobus fulgidus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.2.1.B11 7000
-
 2 * 7000, SDS-PAGE Archaeoglobus fulgidus
6.2.1.B11 7400
-
 2 * 7400, SDS-PAGE Methanocaldococcus jannaschii
6.2.1.B11 72000
-
 2 * 72000, SDS-PAGE Archaeoglobus fulgidus
6.2.1.B11 78172
-
 2 * 78172, calculated from sequence Methanocaldococcus jannaschii
6.2.1.B11 140000
-
 gel filtration Archaeoglobus fulgidus
6.2.1.B11 160000
-
 gel filtration Methanocaldococcus jannaschii

Organism

EC Number Organism UniProt Comment Textmining
6.2.1.B11 Archaeoglobus fulgidus O28341
-
-
6.2.1.B11 Archaeoglobus fulgidus O29057
-
-
6.2.1.B11 Methanocaldococcus jannaschii Q58010
-
-
6.2.1.B11 Methanocaldococcus jannaschii DSM 2661 Q58010
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.2.1.B11 recombinant enzyme Archaeoglobus fulgidus
6.2.1.B11 recombinant enzyme Methanocaldococcus jannaschii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.2.1.B11 ADP + phosphate + acetyl-CoA the enzyme is specific for acetyl-CoA (100%) and butyryl-CoA (120%) but does not take phenylacetyl-CoA (0%). A significant rate of the reverse reaction direction, i.e., the ATP- and CoA-dependent conversion of acetate or butyrate to the corresponding CoA esters, can not be demonstrated Methanocaldococcus jannaschii ATP + acetate + CoA
-
 ir
6.2.1.B11 ADP + phosphate + acetyl-CoA the enzyme is specific for acetyl-CoA (100%) and butyryl-CoA (120%) but does not take phenylacetyl-CoA (0%). A significant rate of the reverse reaction direction, i.e., the ATP- and CoA-dependent conversion of acetate or butyrate to the corresponding CoA esters, can not be demonstrated Methanocaldococcus jannaschii DSM 2661 ATP + acetate + CoA
-
 ir
6.2.1.B11 ADP + phosphate + butyryl-CoA the enzyme is specific for acetyl-CoA (100%) and butyryl-CoA (120%) but does not take phenylacetyl-CoA (0%) Methanocaldococcus jannaschii ATP + butyrate + CoA
-
 ?
6.2.1.B11 ADP + phosphate + butyryl-CoA the enzyme is specific for acetyl-CoA (100%) and butyryl-CoA (120%) but does not take phenylacetyl-CoA (0%) Methanocaldococcus jannaschii DSM 2661 ATP + butyrate + CoA
-
 ?
6.2.1.B11 ADP + phosphate + indole-3-acetyl-CoA
-
 Archaeoglobus fulgidus ATP + indole-3-acetate + CoA
-
 r
6.2.1.B11 ADP + phosphate + phenylacetyl-CoA
-
 Archaeoglobus fulgidus ATP + phenylacetate + CoA
-
 r
6.2.1.B11 ATP + acetate + CoA activity is 13% compared to activity with phenylacetate. At 1 mM acetyl-CoA, the enzyme activity is less than 2% of the rate obtained with phenylacetyl-CoA Archaeoglobus fulgidus ADP + phosphate + acetyl-CoA
-
 ?
6.2.1.B11 ATP + acetate + CoA GTP is as effective as ATP as a substrate Archaeoglobus fulgidus ADP + phosphate + acetyl-CoA
-
 r
6.2.1.B11 ATP + butyrate + CoA activity is 36% compared to activity with phenylacetate Archaeoglobus fulgidus ADP + phosphate + butyryl-CoA
-
 ?
6.2.1.B11 ATP + butyrate + CoA activity is 84% compared to activity with acetate Archaeoglobus fulgidus ADP + phosphate + butyryl-CoA
-
 r
6.2.1.B11 ATP + fumarate + CoA activity is 10% compared to activity with acetate Archaeoglobus fulgidus ADP + phosphate + fumaryl-CoA
-
 ?
6.2.1.B11 ATP + fumarate + CoA activity is 29% compared to activity with phenylacetate Archaeoglobus fulgidus ADP + phosphate + fumaryl-CoA
-
 ?
6.2.1.B11 ATP + indole-3-acetate + CoA activity is 4% compared to activity with acetate Archaeoglobus fulgidus ADP + phosphate + indole-3-acetyl-CoA
-
 ?
6.2.1.B11 ATP + indole-3-acetate + CoA the enzyme shows the highest activity with the aryl acids, indoleacetate (100%) and phenylacetate (65%), as compared to acetate (10-13%) Archaeoglobus fulgidus ADP + phosphate + indole-3-acetyl-CoA
-
 r
6.2.1.B11 ATP + isobutyrate + CoA activity is 31% compared to activity with phenylacetate Archaeoglobus fulgidus ADP + phosphate + isobutyryl-CoA
-
 ?
6.2.1.B11 ATP + isobutyrate + CoA activity is 56% compared to activity with acetate Archaeoglobus fulgidus ADP + phosphate + isobutyryl-CoA
-
 ?
6.2.1.B11 ATP + isovalerate + CoA activity is 10% compared to activity with acetate Archaeoglobus fulgidus ADP + phosphate + isovaleryl-CoA
-
 ?
6.2.1.B11 ATP + isovalerate + CoA activity is 18% compared to activity with phenylacetate Archaeoglobus fulgidus ADP + phosphate + isovaleryl-CoA
-
 ?
6.2.1.B11 ATP + phenylacetate + CoA activity is 10% compared to activity with acetate Archaeoglobus fulgidus ADP + phosphate + phenylacetyl-CoA
-
 ?
6.2.1.B11 ATP + phenylacetate + CoA the enzyme shows the highest activity with the aryl acids, indoleacetate (100%) and phenylacetate (65%), as compared to acetate (10-13%). ATP (100%) is effectively replaced by GTP (70%) Archaeoglobus fulgidus ADP + phosphate + phenylacetyl-CoA
-
 r
6.2.1.B11 ATP + propionate + CoA activity is 42% compared to activity with phenylacetate Archaeoglobus fulgidus ADP + phosphate + propionyl-CoA
-
 ?
6.2.1.B11 ATP + propionate + CoA propionate is as effective as acetate as substrate Archaeoglobus fulgidus ADP + phosphate + propionyl-CoA
-
 r
6.2.1.B11 ATP + succinate + CoA activity is 9% compared to activity with acetate Archaeoglobus fulgidus ADP + phosphate + succinyl-CoA
-
 ?
6.2.1.B11 GTP + acetate + CoA GTP is as effective as ATP as a substrate Archaeoglobus fulgidus GDP + phosphate + acetyl-CoA
-
 r
6.2.1.B11 GTP + indole-3-acetate + CoA ATP (100%) is effectively replaced by GTP (70%) Archaeoglobus fulgidus GDP + phosphate + indole-3-acetyl-CoA
-
 ?
6.2.1.B11 GTP + phenylacetate + CoA ATP (100%) is effectively replaced by GTP (70%) Archaeoglobus fulgidus GDP + phosphate + phenylacetyl-CoA
-
 ?

Subunits

EC Number Subunits Comment Organism
6.2.1.B11 homodimer 2 * 72000, SDS-PAGE Archaeoglobus fulgidus
6.2.1.B11 homodimer 2 * 7000, SDS-PAGE Archaeoglobus fulgidus
6.2.1.B11 homodimer 2 * 7400, SDS-PAGE Methanocaldococcus jannaschii
6.2.1.B11 homodimer 2 * 78172, calculated from sequence Methanocaldococcus jannaschii

Synonyms

EC Number Synonyms Comment Organism
6.2.1.B11 acetyl CoA synthetase (ADP forming)
-
 Archaeoglobus fulgidus
6.2.1.B11 acetyl CoA synthetase (ADP forming)
-
 Methanocaldococcus jannaschii
6.2.1.B11 acetyl coenzyme A synthetase (ADP forming)
-
 Archaeoglobus fulgidus
6.2.1.B11 acetyl coenzyme A synthetase (ADP forming)
-
 Methanocaldococcus jannaschii
6.2.1.B11 ADP-forming acetyl coenzyme A synthetase
-
 Archaeoglobus fulgidus
6.2.1.B11 ADP-forming acetyl coenzyme A synthetase
-
 Methanocaldococcus jannaschii
6.2.1.B11 AF1211 locus name Archaeoglobus fulgidus
6.2.1.B11 AF1938 locus name Archaeoglobus fulgidus
6.2.1.B11 MJ0590 locus name Methanocaldococcus jannaschii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.2.1.B11 55
-
 assay at Methanocaldococcus jannaschii
6.2.1.B11 77
-
-
 Archaeoglobus fulgidus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
6.2.1.B11 60 80 60°C: about 55% of maximal activity, 80°C: 80% of maximal activity Archaeoglobus fulgidus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
6.2.1.B11 70
-
 5 h, about 30% loss of activity Archaeoglobus fulgidus
6.2.1.B11 80
-
 150 min, about 65% loss of activity Archaeoglobus fulgidus
6.2.1.B11 85
-
 30 min, about 80% loss of activity. Almost complete loss of activity after 100 min Archaeoglobus fulgidus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.2.1.B11 1.84
-
 acetate pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 2.3
-
 phenylacetyl-CoA pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 2.9
-
 CoA pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 3
-
 ATP pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 3
-
 phenylacetate pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 3.45
-
 indole-3-acetate pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 11.5
-
 phenylacetate pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 58
-
 phosphate pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 70
-
 ADP pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 95
-
 acetyl-CoA pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 110
-
 CoA pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 138
-
 acetate pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 150
-
 ATP pH 8.0, 55°C Archaeoglobus fulgidus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.2.1.B11 7
-
-
 Archaeoglobus fulgidus
6.2.1.B11 8
-
 assay at Methanocaldococcus jannaschii
6.2.1.B11 8
-
 assay at Archaeoglobus fulgidus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
6.2.1.B11 6 8 about 50% of the maximal activity is found at pH 6 and 8 Archaeoglobus fulgidus

General Information

EC Number General Information Comment Organism
6.2.1.B11 physiological function the enzyme is involved in acetate formation and energy conservation Methanocaldococcus jannaschii
6.2.1.B11 physiological function the enzyme is involved in acetate formation and energy conservation Archaeoglobus fulgidus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
6.2.1.B11 0.7
-
 acetate pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 1.2
-
 phenylacetate pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 2.7
-
 indole-3-acetate pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 5.4
-
 CoA pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 100
-
 ATP pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 111
-
 phenylacetate pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 140
-
 phenylacetyl-CoA pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 400
-
 acetate pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 520
-
 phosphate pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 1120
-
 ATP pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 4000
-
 CoA pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 9200
-
 acetyl-CoA pH 8.0, 55°C Archaeoglobus fulgidus
6.2.1.B11 10000
-
 ADP pH 8.0, 55°C Archaeoglobus fulgidus