Any feedback?
Please rate this page
(search_result.php)
(0/150)

BRENDA support

Refine search

Search General Information

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search

Search term:

Results 1 - 9 of 9
EC Number General Information Commentary Reference
Show all pathways known for 1.5.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.1evolution enzyme Pyr2C reductase is a member of the ornithine cyclodeaminase/micro-crystallin superfamily, different from known dpkA protein, and there are several significant differences in the enzymatic properties between Azospirillum brasilense and another bacteria: substrate and coenzyme specificities, phylogenetic analysis 742531
Show all pathways known for 1.5.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.1evolution enzymes that reduce DELTA1-pyrroline-5-carboxylate and DELTA1-piperideine-6-carboxylate are aldimine reductases whereas enzymes that reduce DELTA1-piperideine-2-carboxylate and DELTA1-pyrroline-2-carboxylate (P2C/Pyr2C) are ketimine reductases (KRs) 743355
Show all pathways known for 1.5.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.1malfunction disruption of LhpI gene from Azospirillum brasilense leads to loss of growth on trans-3-hydroxy-L-proline (T3LHyp), D-proline and D-lysine 742531
Show all pathways known for 1.5.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.1malfunction disruption of LhpI gene from Azospirillum brasilense leads to loss of growth on trans-3-hydroxy-L-proline, D-proline and D-lysine, indicating that this gene has dual metabolic functions as a reductase for Pyr2C and DELTA1-piperidine-2-carboxylate in these pathways, and that the T3LHyp pathway is not linked to trans-4-hydroxy-L-proline and L-proline metabolism 742531
Show all pathways known for 1.5.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.1metabolism lysine degradation may be divided into two distinct pathways, namely (1) the pipecolate pathway which involves oxidation at the alpha-amino position followed by reduction of the product (P2C) to pipecolate by ketimine reductase (KR), and (2) the saccharopine pathway which involves oxidation at the epsilon-amino position The saccharopine pathway is predominantly mitochondrial, whereas the pipecolate pathway is predominantly cytosolic (but with a portion occurring in the peroxisomes). The DELTA1-piperideine-2-carboxylate (P2C) reductase enzyme activity is potently inhibited by thyroid hormones, thus suggesting a reciprocal relationship between enzyme catalysis and thyroid hormone bioavailability. KR is involved in a number of amino acid metabolic pathways. As DELTA1-piperideine-2-carboxylate (P2C) reductase it plays a role in the pipecolate pathway of lysine metabolism. Potent regulation of KR activity by thyroid hormones. KR is also involved in L-ornithine/L-glutamate/L-proline metabolism as well as sulfur-containing amino acid metabolism. Unique presence of the pipecolate pathway in brain. Cerebral pipecolate pathway, overview 743355
Show all pathways known for 1.5.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.1metabolism the enzyme is involved in the trans-3-hydroxy-L-proline pathway and the metabolic networks with D-lysine and D-proline, overview. The trans-3-hydroxy-L-proline pathway is not linked to trans-4-hydroxy-L-proline and L-proline metabolism 742531
Show all pathways known for 1.5.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.1physiological function enzyme AbLhpI is a bifunctional NAD(P)H-dependent Delta1-pyrroline-2-carboxylate/Delta1-piperideine-2-carboxylate reductase (Pyr2C/Pip2C reductase) 742531
Show all pathways known for 1.5.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.1physiological function identification of ketimine reductase (KR) as mu-crystalin (CRYM)/cytosolic thyroid hormone binding protein (THBP). CRYM is a major mammalian THBP, which has the ability to strongly bind thyroid hormones in an NADPH-dependent fashion. It is also active as a DELTA1-piperideine-2-carboxylate (P2C) reductase, which catalyzes the NAD(P)H-dependent reduction of -C=N- (imine) double bonds of a number of cyclic ketimine substrates including sulfur-containing cyclic ketimines. P2C exists in equilibrium with its open-chain form under acidic conditions, but at neutral pH, P2C exists predominantly as the enzymatically favorable cyclic ketimine form (in which the ring double bond is in the C=N form). P2C can also exist as an enamine, but only at basic pH values. The enzyme activity is potently inhibited by thyroid hormones, thus suggesting a reciprocal relationship between enzyme catalysis and thyroid hormone bioavailability. KR is involved in a number of amino acid metabolic pathways. As DELTA1-piperideine-2-carboxylate (P2C) reductase it plays a role in the pipecolate pathway of lysine metabolism. Potent regulation of KR activity by thyroid hormones. KR is also involved in L-ornithine/L-glutamate/L-proline metabolism as well as sulfur-containing amino acid metabolism. Although KR is important in the formation of L-pipecolate in the brain, it is also an important source of L-proline. This proline (via proline oxidase) in turn is an important source of DELTA1-pyrroline-5-carboxylate (Pyr5C) and hence of glutamate and to a lesser extent ornithine. Ketimine reductase is involved in several diseases 743355
Show all pathways known for 1.5.1.1Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.1physiological function the enzymatic reduction of Pyr2C to L-proline together with DAAO may be regarded as a salvage mechanism for converting D-proline, arising from the diet or intestinal bacteria, to L-proline, the more biological useful enantiomer in mammals 743353
Results 1 - 9 of 9