| Literature DB >> 3129020 |
M I Prieto1, J Martin, R Balaña-Fouce, A Garrido-Pertierra.
Abstract
gamma-Aminobutyraldehyde dehydrogenase from Escherichia coli K-12 has been purified and characterized from cell mutants able to grow in putrescine as the sole carbon and nitrogen source. The enzyme has an Mr of 195,000 +/- 10,000 in its dimeric form with an Mr of 95,000 +/- 1,000 for each subunit, a pH optimum at 5.4 in sodium citrate buffer, and does not require bivalent cations for its activity. Km values are 31.3 +/- 6.8 microM and 53.8 +/- 7.4 microM for delta-1-pyrroline and NAD+, respectively. An inhibitory capacity for NADH is also shown using the purified enzyme.Entities:
Mesh：
Substances：
Year: 1987 PMID： 3129020 DOI： 10.1016/0300-9084(87)90142-8
Source DB: PubMed Journal: Biochimie ISSN： 0300-9084 Impact factor: 4.079