Resolution and complementation of the labile L-leucine-pyruvate transaminase. An intermediate during enzyme formation under nitrogen starvation in Gluconobacter suboxydans.
L-Leucine-pyruvate transaminase (mol. wt. 70 000) in Gluconobactersuboxydans synthesized during nitrogen starvation contained a labile form which changed to the stable one later. The labile enzyme (mol. wt. 70 000) dissocated to the two proteinaceous components: a cationic one (mol. wt. 10 000--20 000) and an anionic one (mol. wt. 50 000--60 000), during column chromatography on DEAE-cellulose. The enzyme activity was reconstructed when they were mixed. The reconstructed enzyme had almost the same molecular size and enzymatic properties as the labile and the native stable enzymes.
D004355:Drug Stability; D007930:Leucine; D046911:Macromolecular Substances; D008970:Molecular Weight; D009584:Nitrogen / Q000378:metabolism*; D011548:Pseudomonadaceae / Q000201:enzymology / Q000378:metabolism*; D011773:Pyruvates; D000637:Transaminases / Q000302:isolation & purification / Q000378:metabolism
D046911:Macromolecular Substances; D011773:Pyruvates; D000637:Transaminases; C021510:leucine-pyruvate transaminase; D007930:Leucine; D009584:Nitrogen