ENZYME entry: EC 1.2.1.19
| Accepted Name |
| Aminobutyraldehyde dehydrogenase.
|
| Alternative Name(s) |
| 1-pyrroline dehydrogenase. |
| 4-aminobutanal dehydrogenase. |
| ABALDH. |
| Gamma-guanidinobutyraldehyde dehydrogenase. |
| Reaction catalysed |
| 4-aminobutanal + NAD(+) + H(2)O <=> 4-aminobutanoate + NADH |
| Comment(s) |
- The enzyme from some species exhibits broad substrate specificity and
has a marked preference for straight-chain aldehydes (up to 7 carbon
atoms) as substrates.
- The plant enzyme also acts on 4-guanidinobutanal (cf. EC 1.2.1.54).
- As 1-pyrroline and 4-aminobutanal are in equilibrium and can be
interconverted spontaneously, 1-pyrroline may act as the starting
substrate.
- Formerly EC 1.5.1.35.
|
| Cross-references |
| PROSITE | PDOC00068 |
| BRENDA | 1.2.1.19 |
| EC2PDB | 1.2.1.19 |
| ExplorEnz | 1.2.1.19 |
| PRIAM enzyme-specific profiles | 1.2.1.19 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.2.1.19 |
| IUBMB Enzyme Nomenclature | 1.2.1.19 |
| IntEnz | 1.2.1.19 |
| MEDLINE | Find literature relating to 1.2.1.19 |
| MetaCyc | 1.2.1.19 |
| UniProtKB/Swiss-Prot |
| A8AGJ9, ABDH_CITK8; | A7ZLN7, ABDH_ECO24; | B7URJ0, ABDH_ECO27; |
| B7MMS8, ABDH_ECO45; | B7L6F9, ABDH_ECO55; | Q8X9W5, ABDH_ECO57; |
| B5Z0W0, ABDH_ECO5E; | B7MUN0, ABDH_ECO81; | B7LZ33, ABDH_ECO8A; |
| C4ZVI3, ABDH_ECOBW; | B1XDF5, ABDH_ECODH; | A8A002, ABDH_ECOHS; |
| A1AB46, ABDH_ECOK1; | Q0THX6, ABDH_ECOL5; | Q8FHK7, ABDH_ECOL6; |
| B1IS15, ABDH_ECOLC; | P77674, ABDH_ECOLI; | B7N4K1, ABDH_ECOLU; |
| B6IAI9, ABDH_ECOSE; | B1LFH3, ABDH_ECOSM; | Q1RBX3, ABDH_ECOUT; |
| A4WAR9, ABDH_ENT38; | Q6D6Y7, ABDH_ERWCT; | B7LR95, ABDH_ESCF3; |
| C6DD82, ABDH_PECCP; | A9MQY3, ABDH_SALAR; | Q57P61, ABDH_SALCH; |
| Q5PHV8, ABDH_SALPA; | A9MYQ4, ABDH_SALPB; | C0Q4N4, ABDH_SALPC; |
| Q8Z747, ABDH_SALTI; | Q8ZPC9, ABDH_SALTY; | A8GHZ8, ABDH_SERP5; |
| Q32FQ5, ABDH_SHIDS; | Q0T431, ABDH_SHIF8; | Q83R90, ABDH_SHIFL; |
| Q3Z1H6, ABDH_SHISS; | P49189, AL9A1_HUMAN; |
|
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