Reaction participants Show >> << Hide
- Name help_outline L-aspartate Identifier CHEBI:29991 Charge -1 Formula C4H6NO4 InChIKeyhelp_outline CKLJMWTZIZZHCS-REOHCLBHSA-M SMILEShelp_outline [NH3+][C@@H](CC([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 71 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline menaquinone-8 Identifier CHEBI:44027 (CAS: 523-38-6) help_outline Charge 0 Formula C51H72O2 InChIKeyhelp_outline LXKDFTDVRVLXFY-WQWYCSGDSA-N SMILEShelp_outline CC(C)=CCC\C(C)=C\CC\C(C)=C\CC\C(C)=C\CC\C(C)=C\CC\C(C)=C\CC\C(C)=C\CC\C(C)=C\CC1=C(C)C(=O)c2ccccc2C1=O 2D coordinates Mol file for the small molecule Search links Involved in 18 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline iminosuccinate Identifier CHEBI:77875 Charge -1 Formula C4H4NO4 InChIKeyhelp_outline NMUOATVLLQEYHI-UHFFFAOYSA-M SMILEShelp_outline [O-]C(=O)CC(=[NH2+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 9 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline menaquinol-8 Identifier CHEBI:61684 Charge 0 Formula C51H74O2 InChIKeyhelp_outline OIEZRVBFVPGODT-WQWYCSGDSA-N SMILEShelp_outline CC(C)=CCC\C(C)=C\CC\C(C)=C\CC\C(C)=C\CC\C(C)=C\CC\C(C)=C\CC\C(C)=C\CC\C(C)=C\Cc1c(C)c(O)c2ccccc2c1O 2D coordinates Mol file for the small molecule Search links Involved in 19 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:29191 | RHEA:29192 | RHEA:29193 | RHEA:29194 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Redox potentials and quinone reductase activity of L-aspartate oxidase from Escherichia coli.
Tedeschi G., Zetta L., Negri A., Mortarino M., Ceciliani F., Ronchi S.
l-Aspartate oxidase (EC 1.4.3.16) is a flavoprotein that catalyzes the first step in the de novobiosynthetic pathway to pyridine nucleotides both under aerobic and under anaerobic conditions. Despite the physiological importance of this biosynthesis particularly in facultative aerobic organisms, s ... >> More
l-Aspartate oxidase (EC 1.4.3.16) is a flavoprotein that catalyzes the first step in the de novobiosynthetic pathway to pyridine nucleotides both under aerobic and under anaerobic conditions. Despite the physiological importance of this biosynthesis particularly in facultative aerobic organisms, such as Escherichia coli, little is known about the electron acceptor of reduced L-aspartate oxidase in the absence of oxygen. In this report, evidence is presented which suggests that in vitro quinones can play such a role. L-Aspartate oxidase binds menadione and 2, 3-dimethoxy-5-methyl-p-benzoquinone with Kd values of 11.5 and 2.4 microM, respectively. A new L-aspartate:quinone oxidoreductase activity is described in the presence and in the absence of phospholipids, and its possible physiological relevance is discussed. Moreover, considering the striking sequence similarity between L-aspartate oxidase and the highly conserved family of succinate-fumarate oxidoreductases, the redox properties of L-aspartate oxidase were investigated in detail. A value of -216 mV was calculated for the midpoint potential of the couple FAD/FADH2 bound to the enzyme. This result perfectly explains why L-aspartate oxidase may be considered as a very particular fumarate reductase unable to use succinate as the electron donor. << Less
Biochemistry 36:16221-16230(1997) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.