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Literature summary for 4.1.3.34 extracted from

  • Aoshima, M.; Ishii, M.; Igarashi, Y.
    A novel enzyme, citryl-CoA lyase, catalysing the second step of the citrate cleavage reaction in Hydrogenobacter thermophilus TK-6 (2004), Mol. Microbiol., 52, 763-770.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
cloned, sequenced and expressed in Escherichia coli BL21(DE3) Hydrogenobacter thermophilus

Inhibitors

Inhibitors Comment Organism Structure
ATP
-
Hydrogenobacter thermophilus
citrate
-
Hydrogenobacter thermophilus
CoA
-
Hydrogenobacter thermophilus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.05
-
acetyl-CoA pH 8.0, 70°C Hydrogenobacter thermophilus
0.082
-
citryl-CoA pH 8.0, 70°C Hydrogenobacter thermophilus
0.13
-
oxaloacetate pH 8.0, 70°C Hydrogenobacter thermophilus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
30000
-
3 * 30000, homotrimer, SDS-PAGE Hydrogenobacter thermophilus
87000
-
gel filtration Hydrogenobacter thermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(3S)-citryl-CoA Hydrogenobacter thermophilus reductive tricarboxylic acid cycle, second step of citrate cleavage reaction acetyl-CoA + oxaloacetate
-
r
(3S)-citryl-CoA Hydrogenobacter thermophilus TK-6 / IAM 12695 reductive tricarboxylic acid cycle, second step of citrate cleavage reaction acetyl-CoA + oxaloacetate
-
r

Organism

Organism UniProt Comment Textmining
Hydrogenobacter thermophilus
-
-
-
Hydrogenobacter thermophilus TK-6 / IAM 12695
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native and recombinant enzyme Hydrogenobacter thermophilus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1
-
citrate synthase activity as a side reaction Hydrogenobacter thermophilus
33
-
citrate, ATP, CoA and citryl-CoA forming enzyme CCS in the enzyme assay Hydrogenobacter thermophilus
280
-
purified citryl-CoA as substrate Hydrogenobacter thermophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(3S)-citryl-CoA
-
Hydrogenobacter thermophilus acetyl-CoA + oxaloacetate
-
r
(3S)-citryl-CoA reductive tricarboxylic acid cycle, second step of citrate cleavage reaction Hydrogenobacter thermophilus acetyl-CoA + oxaloacetate
-
r
(3S)-citryl-CoA
-
Hydrogenobacter thermophilus TK-6 / IAM 12695 acetyl-CoA + oxaloacetate
-
r
(3S)-citryl-CoA reductive tricarboxylic acid cycle, second step of citrate cleavage reaction Hydrogenobacter thermophilus TK-6 / IAM 12695 acetyl-CoA + oxaloacetate
-
r
additional information shows low citrate synthase activity Hydrogenobacter thermophilus ?
-
?
additional information shows low citrate synthase activity Hydrogenobacter thermophilus TK-6 / IAM 12695 ?
-
?

Subunits

Subunits Comment Organism
trimer 3 * 30000, homotrimer, SDS-PAGE Hydrogenobacter thermophilus

Synonyms

Synonyms Comment Organism
CCL
-
Hydrogenobacter thermophilus
citryl-CoA lyase
-
Hydrogenobacter thermophilus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
80 90 thermostable with no detectable loss of activity at 80°C for 10 min, retains 83% after 90°C for 10 min Hydrogenobacter thermophilus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
570
-
citryl-CoA pH 8.0, 70°C Hydrogenobacter thermophilus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8 8.5
-
Hydrogenobacter thermophilus

pH Range

pH Minimum pH Maximum Comment Organism
7 9.5 10% of maximum activity at pH 7.0, 50% of maximum activity at pH 7.5, 90% of maximum activity at pH 9.0, 30% of maximum activity at pH 9.5 Hydrogenobacter thermophilus