EC Number   |
General Information |
Reference |
|---|
    1.1.1.85 | drug target |
since leucine is an essential amino acid for humans, and it is also vital for the growth of many pathogenic bacteria, the enzymes belonging to this pathway can be considered as potential target sites for designing of a new class of antibacterial agents |
-, 762701 |
| 1.1.1.85 | evolution |
for a new phenotypic trait to appear, a genetic mutation is not strictly needed, whereas environmental conditions may play an arbitrary role in enabling or not promiscuous phenotypes. D-malate metabolism is made possible by leucine deprivation, which is a priori unrelated |
-, 763032 |
| 1.1.1.85 | metabolism |
IPMDH1 is the major enzyme that participates in Met chain-elongation pathway |
-, 763704 |
| 1.1.1.85 | metabolism |
IPMDH2 and IPMDH3 are functionally redundant in Leu biosynthesis with IPMDH3 playing a larger role than IPMDH2 |
-, 763704 |
| 1.1.1.85 | metabolism |
leuB plays a very important roles in regulating fatty acid synthesis in Mucor circinelloides |
-, 763179 |
| 1.1.1.85 | metabolism |
the enzyme belongs to the leucine biosynthetic pathway |
-, 762701 |
| 1.1.1.85 | metabolism |
the enzyme is involved in leucine biosynthesis |
-, 762765 |
| 1.1.1.85 | metabolism |
upon leucine starvation, the physiological concentration of the enzyme raises to a level that is sufficient for metabolizing D-malate thanks to substrate promiscuity. Under these conditions, the enzyme must also play its native role in leucine biosynthesis so the enzyme is phenotypically active in two core metabolic pathways at the same time |
-, 763032 |
| 1.1.1.85 | more |
physical interaction between isopropylmalate isomerase (IPMI) and isopropylmalate dehydrogenases (IPMDHs) in planta. Because the anti-IPMDH antibody recognizes all three IPMDHs, it is not certain which IPMDHs actually interact with LeuC in planta. The complex formation may represent a new regulatory mechanism controlling Met chain-elongation and/or Leu biosynthesis |
-, 763704 |
| 1.1.1.85 | physiological function |
isoforms IPMDH2 and IPMDH3 proteins exhibit significantly higher activity toward 3-isopropylmalate than isoform IPMDH1. Single mutants of isoforms IPMDH2 or IPMDH3 lack a discernible phenotype. A ipmdh2 ipmdh3 double mutant is lethal in male gametophytes and has reduced transmission through female gametophytes. The aborted pollen grains are small, abnormal in cellular structure, and arrested in germination. Half of the double mutant embryo sacs exhibits slowed development. The IPMDH2/ipmdh2 ipmdh3/ipmdh3 genotype exhibits abnormal vegetative phenotypes. This mutant and a triple mutant containing one allele of IPMDH2 or IPMDH3 have decreased leucine biosynthetic enzyme activities and lower free leucine concentrations |
726052 |
