EC Number   |
General Information |
Reference |
|---|
    1.2.1.88 | evolution |
plant GSALDHs of the ALDH12 family share very low sequence identity with bacterial, fungal, and animal GSALDHs (classified as ALDH4), which are the closest related ALDH superfamily members. Nearly all key residues involved in the recognition of GSAL are identical to those in ALDH4, indicating a close functional relationship with ALDH4. Phylogenetic analysis of the ALDH4 and ALDH12 families suggests that the transition from ALDH4 to ALDH12 occurred during the evolution of the endosymbiotic plant ancestor, prior to the evolution of green algae and land plants |
763363 |
| 1.2.1.88 | more |
enzyme structure comparisons |
763363 |
| 1.2.1.88 | physiological function |
ALDH12 encodes an NAD+-dependent glutamate gamma-semialdehyde dehydrogenase (GSALDH), which irreversibly converts glutamate gamma -semialdehyde (GSAL), a mitochondrial intermediate of the proline and arginine catabolism, to glutamate |
763363 |
| 1.2.1.88 | physiological function |
an Escherichia coli DH5alpha transformant with the P5CDH gene secretes organic acid in medium with TCP as the sole source of phosphate. Acetic acid and alpha-ketoglutarate are secreted in 4 and 24 h, respectively. The recombinant expression decreases the pH of the medium from 6.6 to 3.5 and releases soluble phosphate at 0.172 mg/ml in 28 h |
-, 740252 |
| 1.2.1.88 | physiological function |
deletion of delta1-pyrroline-5-carboxylate dehydrogenase gene ycgN increases poly-gamma glutamic acid yield to 13.91 g/l, 85.22% higher than that of the wild type. Deletion of proline dehydrogenase gene ycgM has no effect on poly-gamma glutamic acid synthesis. A 2.92fold higher delta1-pyrroline-5-carboxylate content (19.24 micromol per g dry cell weight) is detected in the ycgN deficient strain. The ROS level of of the deletion strain is increased by 1.18fold, and addition of N-acetylcysteine (antioxidant) decreases its ROS level |
762655 |
| 1.2.1.88 | physiological function |
gene is able to complement a yeast strain deficient in PUT2 activity |
-, 740744 |
| 1.2.1.88 | physiological function |
one of three key regulatory enzyme of intestinal citrulline synthesis |
701646 |
| 1.2.1.88 | physiological function |
P5CDH mutants activate pro dehydrogenase as wild type plants. They achieve maximum oxidative burst and cell death levels producing normal hypersensitive response lesions, but evidence premature defense activation. The absence of P5CDH does not reduce reactive oxygen species, cell death, or pathogen resistance |
740238 |
