lpdG - Pseudomonas aeruginosa PAO1
lipoamide dehydrogenase-glc
> lpdG - Pseudomonas aeruginosa PAO1 [lipoamide dehydrogenase-glc]
请在左侧输入序列并点击“更新视图”...
统计信息
序列长度
0
疏水性残基
0
极性残基
0
Legend
Metadata
Organism Source: 208964 - Pseudomonas aeruginosa PAO1
EC Number: 1.8.1.4
Cluster:
Registry Model:
Reactions
| reaction id | name | note |
|---|---|---|
| KEGG:R01698 | dihydrolipoamide:NAD+ oxidoreductase | Dihydrolipoamide + NAD+ <=> Lipoamide + NADH + H+ |
| KEGG:R03815 | dihydrolipoylprotein:NAD+ oxidoreductase | a part step of glycine cleavage system (see R01221, R03425+R04125+R03815) |
| KEGG:R07618 | enzyme N6-(dihydrolipoyl)lysine:NAD+ oxidoreductase | Oxo-acid dehydrogenase complexes, dihydrolipoyl dehydrogenase |
| KEGG:R08550 | protein N6-(dihydrolipoyl)lysine:NAD+ oxidoreductase | general reaction (see R03815 and R07618) |
| BioCyc:RXN0-1132 | Pyruvate-dehydrogenase-dihydrolipoate + NAD --> Pyruvate-dehydrogenase-lipoate + NADH + PROTON | |
| BioCyc:RXN-8629 | DIHYDROLIPOYL-GCVH + NAD<=>PROTEIN-LIPOYLLYSINE + NADH + PROTON | |
| BioCyc:1.8.1.4-RXN | Dihydro-Lipoyl-Proteins + NAD --> Lipoyl-Protein-N6-lipoyllysine + NADH + PROTON | |
| BioCyc:RXN-7716 | Oxo-glutarate-dehydrogenase-DH-lipoyl + NAD --> Oxo-glutarate-dehydrogenase-lipoyl + NADH + PROTON | |
| Rhea:RHEA:15046 | N6-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD+ => N6-[(R)-lipoyl]-L-lysyl-[protein] + NADH + H+ | |
| Rhea:RHEA:15047 | N6-[(R)-lipoyl]-L-lysyl-[protein] + NADH + H+ => N6-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD+ | |
| Rhea:RHEA:15048 | N6-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD+ <=> N6-[(R)-lipoyl]-L-lysyl-[protein] + NADH + H+ | |
| Rhea:RHEA:33060 | (R)-dihydrolipoamide + NAD+ => (R)-lipoamide + NADH + H+ | |
| Rhea:RHEA:33061 | (R)-lipoamide + NADH + H+ => (R)-dihydrolipoamide + NAD+ | |
| Rhea:RHEA:33062 | (R)-dihydrolipoamide + NAD+ <=> (R)-lipoamide + NADH + H+ | |
| BioCyc:RXN-7719 | BCAA-dehydrogenase-DH-lipoyl + NAD<=>BCAA-dehydrogenase-lipoyl + NADH + PROTON | A flavoprotein (FAD). A component of the multienzyme 2-oxo-acid dehydrogenase complexes. In the pyruvate dehydrogenase complex, it binds to the core of |FRAME: RXN0-1133 "EC 2.3.1.12, dihydrolipoyllysine-residue acetyltransferase"|, and catalyses oxidation of its dihydrolipoyl groups. It plays a similar role in the oxoglutarate and 3-methyl-2-oxobutanoate dehydrogenase complexes. Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system (click here for diagram), in which it acts, together with |FRAME: GCVP-RXN "EC 1.4.4.2, glycine dehydrogenase (decarboxylating)"|, and |FRAME: GCVT-RXN "EC 2.1.2.10, aminomethyltransferase"|, to break down glycine. It can also use free dihydrolipoate, dihydrolipoamide or dihydrolipoyllysine as substrate. This enzyme was first shown to catalyse the oxidation of NADH by methylene blue; this activity was called diaphorase. The glycine cleavage system is composed of four components that only loosely associate: the P protein (|FRAME: GCVP-RXN "EC 1.4.4.2"|), the T protein (|FRAME: GCVT-RXN "EC 2.1.2.10"|), the L protein (|FRAME: 1.8.1.4-RXN "EC 1.8.1.4"|) and the lipoyl-bearing H protein |CITS: [15642479]|. |
Pathways
| pathway id | name |
|---|