Enzymes
UniProtKB help_outline | 19,337 proteins |
Enzyme class help_outline |
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GO Molecular Function help_outline |
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Reaction participants Show >> << Hide
- 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 20 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 9,134 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)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase]
Identifier
RHEA-COMP:10488
Reactive part
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- 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 12 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline CO2 Identifier CHEBI:16526 (Beilstein: 1900390; 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 977 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-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase]
Identifier
RHEA-COMP:10489
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
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.
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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.
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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 6 other entries.