Enzymes
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Namehelp_outline
N6-[(R)-lipoyl]-L-lysyl-[protein]
Identifier
RHEA-COMP:10474
Reactive part
help_outline
- Name help_outline N6-[(R)-lipoyl]-L-lysine residue Identifier CHEBI:83099 Charge 0 Formula C14H24N2O2S2 SMILEShelp_outline *-N[C@@H](CCCCNC(=O)CCCC[C@@H]1CCSS1)C(-*)=O 2D coordinates Mol file for the small molecule Search links Involved in 20 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 3-methyl-2-oxobutanoate Identifier CHEBI:11851 Charge -1 Formula C5H7O3 InChIKeyhelp_outline QHKABHOOEWYVLI-UHFFFAOYSA-M SMILEShelp_outline CC(C)C(=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 24 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 10,232 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
N6-[(R)-S8-2-methylpropanoyldihydrolipoyl]-L-lysyl-[protein]
Identifier
RHEA-COMP:10497
Reactive part
help_outline
- Name help_outline N6-[(R)-S8-2-methylpropanoyldihydrolipoyl]-L-lysine residue Identifier CHEBI:83142 Charge 0 Formula C18H32N2O3S2 SMILEShelp_outline CC(C)C(=O)SCC[C@H](S)CCCCC(=O)NCCCC[C@H](N-*)C(-*)=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline CO2 Identifier CHEBI:16526 (CAS: 124-38-9) help_outline Charge 0 Formula CO2 InChIKeyhelp_outline CURLTUGMZLYLDI-UHFFFAOYSA-N SMILEShelp_outline O=C=O 2D coordinates Mol file for the small molecule Search links Involved in 1,073 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:13457 | RHEA:13458 | RHEA:13459 | RHEA:13460 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Branched chain alpha-keto acid metabolism. I. Isolation, purification, and partial characterization of bovine liver alpha-ketoisocaproic:alpha-keto-beta-methylvaleric acid dehydrogenase.
Connelly J.L., Danner D.J., Bowden J.A.
J Biol Chem 243:1198-1203(1968) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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Branched chain alpha-keto acid metabolism. II. Evidence for the common identity of alpha-ketoisocaproic acid and alpha-keto-beta-methyl-valeric acid dehydrogenases.
Bowden J.A., Connelly J.L.
J. Biol. Chem. 243:3526-3531(1968) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions.
Perham R.N.
Multistep chemical reactions are increasingly seen as important in a growing number of complex biotransformations. Covalently attached prosthetic groups or swinging arms, and their associated protein domains, are essential to the mechanisms of active-site coupling and substrate channeling in a num ... >> More
Multistep chemical reactions are increasingly seen as important in a growing number of complex biotransformations. Covalently attached prosthetic groups or swinging arms, and their associated protein domains, are essential to the mechanisms of active-site coupling and substrate channeling in a number of the multifunctional enzyme systems responsible. The protein domains, for which the posttranslational machinery in the cell is highly specific, are crucially important, contributing to the processes of molecular recognition that define and protect the substrates and the catalytic intermediates. The domains have novel folds and move by virtue of conformationally flexible linker regions that tether them to other components of their respective multienzyme complexes. Structural and mechanistic imperatives are becoming apparent as the assembly pathways and the coupling of multistep reactions catalyzed by these dauntingly complex molecular machines are unraveled. << Less
Annu Rev Biochem 69:961-1004(2000) [PubMed] [EuropePMC]
This publication is cited by 10 other entries.
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Purification and characterization of branched chain alpha-ketoacid dehydrogenase from bovine liver mitochondria.
Danner D.J., Lemmon S.K., Besharse J.C., Elsas L.J. II
Branched chain alpha-ketoacid dehydrogenase (EC 1.2.4.3(4)) was solubilized and purified from bovine liver mitochondria for the first time. Decarboxylation of alpha-ketoisovalerate, alpha-keto-beta-methylvalerate, and alpha-ketoisocaproate was catalyzed by this multienzyme complex and this activit ... >> More
Branched chain alpha-ketoacid dehydrogenase (EC 1.2.4.3(4)) was solubilized and purified from bovine liver mitochondria for the first time. Decarboxylation of alpha-ketoisovalerate, alpha-keto-beta-methylvalerate, and alpha-ketoisocaproate was catalyzed by this multienzyme complex and this activity was co-purified for each substrate. Three enzymatic functions were contained in the complex including decarboxylation of the above ketoacids, transacylation of their simple acid derivatives, and reduction of NAD+ as an overall reaction. Product stoichiometry of these three reactions was 1 CO2:1 acyl-CoA:1 NADH. Activity depended upon the addition of thiamin pyrophosphate, CoASH, and NAD+ which were dissociable cofactors. Physically, two active forms of the enzyme complex were found: a 275,000-dalton unit and a 2 x 10(6)-dalton component. Both showed a characteristic flavin spectra and catalyzed all functions of the complex, implying that 10 small units aggregated into the larger unit. The soluble complex as visualized by electron microscopy had a diameter ranging from 12 to 24 nm corresponding to a molecular weight of 2 x 10(6). The size of the native membrane-bound component remains to be determined. << Less
J. Biol. Chem. 254:5522-5526(1979) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.