Enzymes
| UniProtKB help_outline | 1 proteins |
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Name help_outline
a plastoquinone
Identifier
CHEBI:17757
(CAS: 112055-76-2)
help_outline
Charge
0
Formula
C8H8O2(C5H8)n
Search links
Involved in 14 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
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Identifier: RHEA-COMP:9562Polymer name: a plastoquinonePolymerization index help_outline nFormula C8H8O2(C5H8)nCharge (0)(0)nMol File for the polymer
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- Name help_outline an L-α-amino acid Identifier CHEBI:59869 Charge 0 Formula C2H4NO2R SMILEShelp_outline [NH3+][C@@H]([*])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 355 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; 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 6,048 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a 2-oxocarboxylate Identifier CHEBI:35179 Charge -1 Formula C2O3R SMILEShelp_outline [O-]C(=O)C([*])=O 2D coordinates Mol file for the small molecule Search links Involved in 586 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Name help_outline
a plastoquinol
Identifier
CHEBI:62192
Charge
0
Formula
C8H10O2(C5H8)n
Search links
Involved in 15 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
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Identifier: RHEA-COMP:9561Polymer name: a plastoquinolPolymerization index help_outline nFormula C8H10O2(C5H8)nCharge (0)(0)nMol File for the polymer
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- Name help_outline NH4+ Identifier CHEBI:28938 (CAS: 14798-03-9) help_outline Charge 1 Formula H4N InChIKeyhelp_outline QGZKDVFQNNGYKY-UHFFFAOYSA-O SMILEShelp_outline [H][N+]([H])([H])[H] 2D coordinates Mol file for the small molecule Search links Involved in 518 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:53020 | RHEA:53021 | RHEA:53022 | RHEA:53023 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Related reactions help_outline
Specific form(s) of this reaction
Publications
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Detection of an L-amino acid dehydrogenase activity in Synechocystis sp. PCC 6803.
Schriek S., Kahmann U., Staiger D., Pistorius E.K., Michel K.P.
The protein Slr0782 from Synechocystis sp. PCC 6803, which has similarity to L-amino acid oxidase from Synechococcus elongatus PCC 6301 and PCC 7942, has been characterized in part. Immunoblot blot analysis showed that Slr0782 is mainly thylakoid membrane-associated. Moreover, expression of slr078 ... >> More
The protein Slr0782 from Synechocystis sp. PCC 6803, which has similarity to L-amino acid oxidase from Synechococcus elongatus PCC 6301 and PCC 7942, has been characterized in part. Immunoblot blot analysis showed that Slr0782 is mainly thylakoid membrane-associated. Moreover, expression of slr0782 mRNA and Slr0782 protein were analyzed and an activity assay was developed. Utilizing toluene-permeabilized cells, an L-arginine-stimulated O(2) uptake became detectable in Synechocystis sp. PCC 6803. Besides oxidizing the basic L-amino acids L-arginine, L-lysine, L-ornithine, and L-histidine, a number of other L-amino acids were also substrates, while D-amino acids were not. The best substrate was L-cysteine, and the second best was L-arginine. The L-arginine-stimulated O(2) uptake was inhibited by cations. The inhibition by o-phenanthroline and salicylhydroxamic acid suggested the presence of a transition metal besides FAD in the enzyme. Moreover, it is shown that inhibitors of the respiratory electron transport chain, such as KCN and 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone, also inhibited the L-arginine-stimulated O(2) uptake, suggesting that Slr0782 functions as an L-arginine dehydrogenase, mediating electron transfer from L-arginine into the respiratory electron transport chain utilizing O(2) as electron acceptor via cytochrome oxidase. The results imply that Slr0782 is an additional substrate dehydrogenase being able to interact with the electron transport chain of the thylakoid membrane. << Less
J. Exp. Bot. 60:1035-1046(2009) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.