Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
citryl-S-ACP lyase
-
-
-
-
CCL
-
citryl-CoA lyase
-
-
additional information
-
EC 4.1.3.6 is a multienzyme complex composed of three proteins: an acyl carrier protein, a citrate,acetate-ACP transferase and a citryl-S-ACP lyase (beta-subunit)
additional information
-
EC 4.1.3.6 is a multienzyme complex composed of three proteins: an acyl carrier protein, a citrate,acetate-ACP transferase and a citryl-S-ACP lyase (beta-subunit)
additional information
-
EC 4.1.3.6 is a multienzyme complex composed of three proteins: an acyl carrier protein, a citrate,acetate-ACP transferase and a citryl-S-ACP lyase (beta-subunit)
additional information
-
EC 4.1.3.6 is a multienzyme complex composed of three proteins: an acyl carrier protein, a citrate,acetate-ACP transferase and a citryl-S-ACP lyase (beta-subunit)
additional information
-
EC 4.1.3.6 is a multienzyme complex composed of three proteins: an acyl carrier protein, a citrate,acetate-ACP transferase and a citryl-S-ACP lyase (beta-subunit)
additional information
-
EC 4.1.3.6 can be dissociated into components, two of which are identical with EC 2.8.3.10 and EC 4.1.3.34
additional information
-
EC 4.1.3.6 is a multienzyme complex composed of three proteins: an acyl carrier protein, a citrate,acetate-ACP transferase and a citryl-S-ACP lyase (beta-subunit)
additional information
-
EC 4.1.3.6 is a multienzyme complex composed of three proteins: an acyl carrier protein, a citrate,acetate-ACP transferase and a citryl-S-ACP lyase (beta-subunit)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(3S)-citryl-CoA
acetyl-CoA + oxaloacetate
(3S)-citryl-[acyl-carrier protein]
acetyl-[acyl-carrier protein] + oxaloacetate
additional information
?
-
(3S)-citryl-CoA
acetyl-CoA + oxaloacetate
-
-
-
?
(3S)-citryl-CoA
acetyl-CoA + oxaloacetate
-
-
-
?
(3S)-citryl-CoA
acetyl-CoA + oxaloacetate
-
-
-
r
(3S)-citryl-CoA
acetyl-CoA + oxaloacetate
-
-
-
?
(3S)-citryl-CoA
acetyl-CoA + oxaloacetate
-
reductive tricarboxylic acid cycle, second step of citrate cleavage reaction
-
r
(3S)-citryl-CoA
acetyl-CoA + oxaloacetate
-
-
-
?
(3S)-citryl-CoA
acetyl-CoA + oxaloacetate
-
-
-
r
(3S)-citryl-CoA
acetyl-CoA + oxaloacetate
-
reductive tricarboxylic acid cycle, second step of citrate cleavage reaction
-
r
(3S)-citryl-CoA
acetyl-CoA + oxaloacetate
-
-
-
?
(3S)-citryl-CoA
acetyl-CoA + oxaloacetate
-
-
-
?
(3S)-citryl-CoA
acetyl-CoA + oxaloacetate
-
-
-
?
(3S)-citryl-CoA
acetyl-CoA + oxaloacetate
-
-
-
?
(3S)-citryl-[acyl-carrier protein]
acetyl-[acyl-carrier protein] + oxaloacetate
-
-
-
?
(3S)-citryl-[acyl-carrier protein]
acetyl-[acyl-carrier protein] + oxaloacetate
-
enzyme is involved in citrate fermentation
-
-
?
additional information
?
-
-
shows low citrate synthase activity
-
?
additional information
?
-
-
shows low citrate synthase activity
-
?
additional information
?
-
-
the enzyme is involved in the biosynthesis of dialkylmaleic anhydride in Streptomyces griseochromogenes
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Co2+
-
absolute requirement for a divalent metal ion: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Co2+
-
absolute requirement for a divalent metal ion: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Co2+
-
absolute requirement for a divalent metal ion: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Co2+
-
absolute requirement for a divalent metal ion: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Co2+
-
absolute requirement for a divalent metal ion: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Co2+
-
absolute requirement for a divalent metal ion: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Co2+
-
absolute requirement for a divalent metal ion: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Fe2+
-
absolute requirement for a divalent metal ion: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Fe2+
-
absolute requirement for a divalent metal ion: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Fe2+
-
absolute requirement for a divalent metal ion: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Fe2+
-
absolute requirement for a divalent metal ion: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Fe2+
-
absolute requirement for a divalent metal ion: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Fe2+
-
absolute requirement for a divalent metal ion: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Fe2+
-
absolute requirement for a divalent metal ion: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Mg2+
-
absolute requirement for a divalent metal ion: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Mg2+
-
absolute requirement for a divalent metal ion: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Mg2+
-
absolute requirement for a divalent metal ion: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Mg2+
-
absolute requirement for a divalent metal ion: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Mg2+
-
absolute requirement for a divalent metal ion: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Mg2+
-
absolute requirement for a divalent metal ion: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Mg2+
-
absolute requirement for a divalent metal ion: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Mn2+
-
absolute requirement for a divalent metal ion: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Mn2+
-
absolute requirement for a divalent metal ion: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Mn2+
-
absolute requirement for a divalent metal ion: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Mn2+
-
absolute requirement for a divalent metal ion: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Mn2+
-
absolute requirement for a divalent metal ion: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Mn2+
-
absolute requirement for a divalent metal ion: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Mn2+
-
absolute requirement for a divalent metal ion: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Zn2+
-
absolute requirement for a divalent metal ion: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Zn2+
-
absolute requirement for a divalent metal ion: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Zn2+
-
absolute requirement for a divalent metal ion: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Zn2+
-
absolute requirement for a divalent metal ion: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Zn2+
-
absolute requirement for a divalent metal ion: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Zn2+
-
absolute requirement for a divalent metal ion: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Zn2+
-
absolute requirement for a divalent metal ion: Mg2+, Mn2+, Zn2+, Fe2+ or Co2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
10000
-
alpha6,beta6,gamma6, 6 * 10000, gamma, + 6 * 33000, beta, + 6 * 55000, alpha
11700
-
alpha6,beta6,gamma6, 6 * 11700, gamma, + 6 * 32000, beta, + 6 * 56000, alpha
12000
-
alpha6,beta6,gamma6, 6 * 12000, gamma, + 6 * 35000, beta, + 6 * 54000, alpha
14000
-
alpha6,beta6,gamma6, 6 * 14000, gamma, + 6 * 37000, beta, + 6 * 54000, alpha
30000
-
3 * 30000, homotrimer, SDS-PAGE
31352
-
x * 31352, determination of amino acid sequence
31600
-
alpha6,beta6,gamma6, 6 + 11400, gamma + 6 * 31600, beta, + 6 * 44600, gamma
33000
-
alpha6,beta6,gamma6, 6 * 10000, gamma, + 6 * 33000, beta, + 6 * 55000, alpha
33354
-
x * 33354, calculation from nucleotide sequence
35000
-
alpha6,beta6,gamma6, 6 * 12000, gamma, + 6 * 35000, beta, + 6 * 54000, alpha
37000
-
alpha6,beta6,gamma6, 6 * 14000, gamma, + 6 * 37000, beta, + 6 * 54000, alpha
44600
-
alpha6,beta6,gamma6, 6 + 11400, gamma + 6 * 31600, beta, + 6 * 44600, gamma
55000
-
alpha6,beta6,gamma6, 6 * 10000, gamma, + 6 * 33000, beta, + 6 * 55000, alpha
56000
-
alpha6,beta6,gamma6, 6 * 11700, gamma, + 6 * 32000, beta, + 6 * 56000, alpha
85000
-
alpha6beta6gamm1, 6 * 32000, acyllyase beta-subunit, + 6 * 54000, acyltransferase alpha-subunit + 1 * 85000, acyl-carrier-protein gamma-subunit, SDS-PAGE
32000
-
alpha6beta6gamm1, 6 * 32000, acyllyase beta-subunit, + 6 * 54000, acyltransferase alpha-subunit + 1 * 85000, acyl-carrier-protein gamma-subunit, SDS-PAGE
32000
-
alpha6,beta6,gamma6, 6 * 11700, gamma, + 6 * 32000, beta, + 6 * 56000, alpha
54000
-
alpha6,beta6,gamma6, 6 * 12000, gamma, + 6 * 35000, beta, + 6 * 54000, alpha
54000
-
alpha6beta6gamm1, 6 * 32000, acyllyase beta-subunit, + 6 * 54000, acyltransferase alpha-subunit + 1 * 85000, acyl-carrier-protein gamma-subunit, SDS-PAGE
54000
-
alpha6,beta6,gamma6, 6 * 14000, gamma, + 6 * 37000, beta, + 6 * 54000, alpha
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
?
-
-
?
-
x * 31352, determination of amino acid sequence
?
-
x * 31352, determination of amino acid sequence
-
?
-
x * 33354, calculation from nucleotide sequence
trimer
-
3 * 30000, homotrimer, SDS-PAGE
trimer
-
3 * 30000, homotrimer, SDS-PAGE
-
additional information
-
EC 4.1.3.6 is a multienzyme complex composed of three proteins: an acyl carrier protein, a citrate,acetate-ACP transferase and a citryl-S-ACP lyase, i.e. beta-subunit
additional information
-
the enzyme is the beta-subunit of EC 4.1.3.6
additional information
-
alpha6,beta6,gamma6, 6 * 14000, gamma, + 6 * 37000, beta, + 6 * 54000, alpha
additional information
-
EC 4.1.3.6 is a multienzyme complex composed of three proteins: an acyl carrier protein, a citrate,acetate-ACP transferase and a citryl-S-ACP lyase, i.e. beta-subunit
additional information
-
the enzyme is the beta-subunit of EC 4.1.3.6
additional information
-
EC 4.1.3.6 is a multienzyme complex composed of three proteins: an acyl carrier protein, a citrate,acetate-ACP transferase and a citryl-S-ACP lyase, i.e. beta-subunit
additional information
-
the enzyme is the beta-subunit of EC 4.1.3.6
additional information
-
alpha6beta6gamm1, 6 * 32000, acyllyase beta-subunit, + 6 * 54000, acyltransferase alpha-subunit + 1 * 85000, acyl-carrier-protein gamma-subunit, SDS-PAGE
additional information
-
EC 4.1.3.6 is a multienzyme complex composed of three proteins: an acyl carrier protein, a citrate,acetate-ACP transferase and a citryl-S-ACP lyase, i.e. beta-subunit
additional information
-
the enzyme is the beta-subunit of EC 4.1.3.6
additional information
-
alpha6,beta6,gamma6, 6 * 11700, gamma, + 6 * 32000, beta, + 6 * 56000, alpha
additional information
-
EC 4.1.3.6 is a multienzyme complex composed of three proteins: an acyl carrier protein, a citrate,acetate-ACP transferase and a citryl-S-ACP lyase, i.e. beta-subunit
additional information
-
the enzyme is the beta-subunit of EC 4.1.3.6
additional information
-
alpha6,beta6,gamma6, 6 * 12000, gamma, + 6 * 35000, beta, + 6 * 54000, alpha
additional information
-
EC 4.1.3.6 is a multienzyme complex composed of three proteins: an acyl carrier protein, a citrate,acetate-ACP transferase and a citryl-S-ACP lyase, i.e. beta-subunit
additional information
-
the enzyme is the beta-subunit of EC 4.1.3.6
additional information
-
the enzyme is the beta-subunit of EC 4.1.3.6
additional information
-
alpha6,beta6,gamma6, 6 * 10000, gamma, + 6 * 33000, beta, + 6 * 55000, alpha
additional information
-
EC 4.1.3.6 is a multienzyme complex composed of three proteins: an acyl carrier protein, a citrate,acetate-ACP transferase and a citryl-S-ACP lyase, i.e. beta-subunit
additional information
-
the enzyme is the beta-subunit of EC 4.1.3.6
additional information
-
alpha6,beta6,gamma6, 6 + 11400, gamma + 6 * 31600, beta, + 6 * 44600, gamma
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Bekal, S.; van Beeumen, J.; Samyn, B.; Garmyn, D.; Henini, S.; Divies, C.; Prevost, H.
Purification of Leuconostoc mesenteroides citrate lyase and cloning and characterization of the citCDEFG gene cluster
J. Bacteriol.
180
647-654
1998
Leuconostoc mesenteroides
brenda
Hupperich, M.; Henschen, A.; Eggerer, H.
Citrate lyase from Klebsiella pneumoniae. The complete primary structure of the acyl lyase subunit
Eur. J. Biochem.
192
161-166
1990
Klebsiella pneumoniae, Klebsiella pneumoniae ATCC 13882
brenda
Man, W.J.; Li, Y.; O'Connor, C.D.; Wilton, D.C.
Conversion of citrate synthase into citryl-CoA lyase as a result of mutation of the active-site aspartic acid residue to glutamic acid
Biochem. J.
280
521-526
1991
Escherichia coli
brenda
Bekal, S.; Divies, C.; Prevost, H.
Citrate lyases of lactic acid bacteria
Lait
78
3-10
1998
Leuconostoc mesenteroides, Lacrimispora sphenoides, Escherichia coli, Enterococcus faecalis, Klebsiella pneumoniae, Lactococcus lactis subsp. lactis, Rubrivivax gelatinosus
-
brenda
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
brenda
Hugler, M.; Huber, H.; Molyneaux, S.J.; Vetriani, C.; Sievert, S.M.
Autotrophic CO2 fixation via the reductive tricarboxylic acid cycle in different lineages within the phylum Aquificae: Evidence for two ways of citrate cleavage
Environ. Microbiol.
9
81-92
2007
Hydrogenobacter hydrogenophilus (A1Y9I4), Sulfurihydrogenibium subterraneum (A1Y9I5), Thermocrinis ruber (A1Y9I6)
brenda
Wang, F.; Kong, R.; Liu, B.; Zhao, J.; Qiu, R.; Tang, L.
Functional characterization of the genes tauO, tauK, and tauI in the biosynthesis of tautomycetin
J. Microbiol.
50
770-776
2012
Streptomyces griseochromogenes
brenda
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)
brenda