A pyridoxal 5'-phosphate protein . The product, 4-aminobutanal, spontaneously cyclizes to form 1-pyrroline, which may be the actual substrate for EC 1.2.1.19, aminobutyraldehyde dehydrogenase. Cadaverine and spermidine can also act as substrates . Forms part of the arginine-catabolism pathway . cf. EC 2.6.1.113, putrescine---pyruvate transaminase.
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SYSTEMATIC NAME
IUBMB Comments
putrescine:2-oxoglutarate aminotransferase
A pyridoxal 5'-phosphate protein [3]. The product, 4-aminobutanal, spontaneously cyclizes to form 1-pyrroline, which may be the actual substrate for EC 1.2.1.19, aminobutyraldehyde dehydrogenase. Cadaverine and spermidine can also act as substrates [3]. Forms part of the arginine-catabolism pathway [2]. cf. EC 2.6.1.113, putrescine---pyruvate transaminase.
a knockout mutation in alternative sigma factor, rpoS, abolishes putrescine-dependent ygjG-lacZ expression. RpoS overexpression induces ygjG-lacZ expression with putrescine supplementation but not without supplementation. The loss of putrescine-dependent ygjG-lacZ expression induced by rpoS is completely restored under nitrogen-starvation conditions. The putrescine-dependent expression of ygjG-lacZ under this condition is clearly dependent on alternative sigma factor, rpoN, and its cognate activator ntrC
the N-terminal modification of PATase is generated by a specificity of leucyl/phenylalanyltRNA-protein transferase, in which various combinations of primary destabilising residues (Leu and Phe) are attached to the N-terminal Met. This modification of PATase is essential not only for its recognition by ClpS, but also determines the stability of the protein in vivo
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of YgjG at 2.3 and 2.1 A resolutions for the free and putrescine-bound enzymes, respectively. YgjG forms a dimer that adopts a class III pyridoxal 5'-phosphate-dependent aminotransferase fold. Structures of YgjG and other class III aminotransferases are similar. YgjG has an additional N-terminal helical structure that partially contributes to a dimeric interaction with the other subunit via a helix-helix interaction. The YgjG substrate-binding site entrance size and charge distribution are smaller and more hydrophobic than other class III aminotransferases
a route for the production of GABA via putrescine in Corynebacterium glutamicum. A putrescine-producing recombinant Corynebacterium glutamicum strain is converted into a GABA producing strain by heterologous expression of putrescine transaminase PatA and gamma-aminobutyraldehyde dehydrogenase PatD genes from Escherichia coli. The resultant strain produces 5.3 g per l of GABA. GABA production is improved further by adjusting the concentration of nitrogen in the culture medium, by avoiding the formation of the by-product N-acetylputrescine and by deletion of the genes for GABA catabolism and GABA re-uptake. GABA accumulation by this strain is increased by 5% to 8.0 g per l, and the volumetric productivity is increased to 0.31 g per l and h
enzyme prefers diaminoalkanes as substrates and thereby generates cyclic imines from the omega-amino aldehyde intermediates. The addition of a mild chemical reducing agent rapidly reduces the imine intermediate in situ to furnish a range of N-heterocycle products