Properties of gamma-aminobutyraldehyde dehydrogenase from Escherichia coli.

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.

journal_name

Biochimie

journal_title

Biochimie

authors

Prieto MI,Martin J,Balaña-Fouce R,Garrido-Pertierra A

doi

10.1016/0300-9084(87)90142-8

subject

Has Abstract

pub_date

1987-11-01 00:00:00

pages

1161-8

issue

11-12

eissn

0300-9084

issn

1638-6183

pii

0300-9084(87)90142-8

journal_volume

69

pub_type

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