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Information on EC 4.1.3.34 - citryl-CoA lyase and Organism(s) Hydrogenobacter thermophilus and UniProt Accession D3DG26

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.3 Oxo-acid-lyases
                4.1.3.34 citryl-CoA lyase
IUBMB Comments
The enzyme is a component of EC 4.1.3.6 {[citrate (pro-3S)-lyase]}and EC 2.3.3.8 [ATP citrate synthase]. Also acts on (3S)-citryl thioacyl-carrier protein.
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This record set is specific for:
Hydrogenobacter thermophilus
UNIPROT: D3DG26
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Word Map
The taxonomic range for the selected organisms is: Hydrogenobacter thermophilus
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
citryl-coa lyase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
citryl-CoA lyase
-
-
citryl-S-ACP lyase
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
(3S)-citryl-CoA oxaloacetate-lyase (acetyl-CoA-forming)
The enzyme is a component of EC 4.1.3.6 {[citrate (pro-3S)-lyase]}and EC 2.3.3.8 [ATP citrate synthase]. Also acts on (3S)-citryl thioacyl-carrier protein.
CAS REGISTRY NUMBER
COMMENTARY hide
131095-35-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(3S)-citryl-CoA
acetyl-CoA + oxaloacetate
show the reaction diagram
-
-
-
?
(3S)-citryl-CoA
acetyl-CoA + oxaloacetate
show the reaction diagram
additional information
?
-
-
shows low citrate synthase activity
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(3S)-citryl-CoA
acetyl-CoA + oxaloacetate
show the reaction diagram
-
-
-
?
(3S)-citryl-CoA
acetyl-CoA + oxaloacetate
show the reaction diagram
-
reductive tricarboxylic acid cycle, second step of citrate cleavage reaction
-
r
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05
acetyl-CoA
-
pH 8.0, 70°C
0.082
citryl-CoA
-
pH 8.0, 70°C
0.13
oxaloacetate
-
pH 8.0, 70°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
570
citryl-CoA
-
pH 8.0, 70°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1
-
citrate synthase activity as a side reaction
280
-
purified citryl-CoA as substrate
33
-
citrate, ATP, CoA and citryl-CoA forming enzyme CCS in the enzyme assay
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
-
3 * 30000, homotrimer, SDS-PAGE
87000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
-
3 * 30000, homotrimer, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80 - 90
-
thermostable with no detectable loss of activity at 80°C for 10 min, retains 83% after 90°C for 10 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native and recombinant enzyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned, sequenced and expressed in Escherichia coli BL21(DE3)
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Mol. Microbiol.
52
763-770
2004
Hydrogenobacter thermophilus, Hydrogenobacter thermophilus TK-6 / IAM 12695
Manually annotated by BRENDA team
Becerra, A.; Rivas, M.; Garcia-Ferris, C.; Lazcano, A.; Pereto, J.
A phylogenetic approach to the early evolution of autotrophy the case of the reverse TCA and the reductive acetyl-CoA pathways
Int. Microbiol.
17
91-97
2014
Hydrogenobacter thermophilus (D3DG26), Hydrogenobacter thermophilus DSM 6534 (D3DG26)
Manually annotated by BRENDA team