Enzymes
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Reaction participants Show >> << Hide
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Namehelp_outline
acetyl-[citrate lyase ACP]
Identifier
RHEA-COMP:13710
Reactive part
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- Name help_outline S-acetyl-O-[2'-(5-phosphoribosyl)-3'-dephospho-CoA]-L-serine(3−) residue Identifier CHEBI:137976 Charge -3 Formula C31H46N8O22P3S SMILEShelp_outline O1[C@@H]([C@@H]([C@@H]([C@H]1COP(OC[C@H](N*)C(=O)*)([O-])=O)O)O)O[C@H]2[C@H](N3C4=C(C(=NC=N4)N)N=C3)O[C@H](COP(OP(OCC([C@H](C(NCCC(NCCSC(C)=O)=O)=O)O)(C)C)(=O)[O-])(=O)[O-])[C@H]2O 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,485 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
holo-[citrate lyase ACP]
Identifier
RHEA-COMP:10158
Reactive part
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- Name help_outline O-[2'-(5-phosphoribosyl)-3'-dephospho-CoA]-L-serine residue Identifier CHEBI:82683 Charge -3 Formula C29H44N8O21P3S SMILEShelp_outline CC(C)(COP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O[C@H]2O[C@H](COP([O-])(=O)OC[C@H](N-*)C(-*)=O)[C@@H](O)[C@H]2O)[C@@H]1O)n1cnc2c(N)ncnc12)[C@@H](O)C(=O)NCCC(=O)NCCS 2D coordinates Mol file for the small molecule Search links Involved in 5 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline acetate Identifier CHEBI:30089 (CAS: 71-50-1) help_outline Charge -1 Formula C2H3O2 InChIKeyhelp_outline QTBSBXVTEAMEQO-UHFFFAOYSA-M SMILEShelp_outline CC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 182 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,932 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:13657 | RHEA:13658 | RHEA:13659 | RHEA:13660 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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Citrate lyase deacetylase of Rhodopseudomonas gelatinosa. Isolation of the enzyme and studies on the inhibition by L-glutamate.
Giffhorn F., Rode H., Kuhn A., Gottschalk G.
Citrate lyase deacetylase or acetyl-S-(acyl-carrier protein) enzyme thioester hydrolase (acetate) (EC 3.1.2-), was purified 3100-fold with a yield of 3.8% from cell extracts of Rhodopseudomonas gelatinosa. The final enzyme preparation gave a single protein band upon polyacrylamide-gel electrophore ... >> More
Citrate lyase deacetylase or acetyl-S-(acyl-carrier protein) enzyme thioester hydrolase (acetate) (EC 3.1.2-), was purified 3100-fold with a yield of 3.8% from cell extracts of Rhodopseudomonas gelatinosa. The final enzyme preparation gave a single protein band upon polyacrylamide-gel electrophoresis in the absence or in the presence of sodium dodecylsulfate. The molecular weight of the native enzyme was estimated by gel filtration to be 14 300 +/-1000. Sodium dodecylsulfate/polyacrylamide gel electrophoresis yielded a molecular weight of 7300 +/-600 indicating that the enzyme consisted of two subunits. Citrate lyase deacetylase acted as an S-acetyl enzyme thioesterhydrolase because it catalyzed the conversion of citrate lyase (S-acetyl form) into citrate lyase (sulfhydryl form) and acetate. Citrate lyase deacetylase was strongly inhibited by L-glutamate. The half-maximal inhibitor concentration was 7.5 X 10(-4) M. and a Ki-value of 1.2 X 10(-4) M was determined. The mode of inhibition appeared to be of the linear mixed type. L-Glutamate was bound by citrate lyase deacetylase but not by citrate lyase. The pool concentrations of L-glutamate in R. gelatinosa were 10 mM when citrate was present in substrate amounts and 2.7 mM after total consumption of citrate. Simulation of conditions in vivo using homogeneous enzyme preparations of citrate lyase and citrate lyase deacetylase, and glutamate concentrations of 10 mM and 2.7 mM respectively, revealed that the rate of citrate lyase inactivation increased from 8% within 15 min during growth on citrate to 50% within 15 min in the absence of citrate. << Less