Sandbox Reserved 1760: Difference between revisions

Line 6:

== Function of your protein ==

The protein Ornithine Aminotransferase (OAT), in humans (hOAT), is an enzyme that catalyzes the the transfer of an amino group from L-ornithine(L-Orn) to α-ketoglutarate (α-KG). Its ligand, pyridoxal-5'-phosphate (PLP), is a cofactor of this reaction. An amino group from L-Orn is transferred to PLP which converts it to pyridoxamine phosphate (PMP) and L-Orn is converted to L-glutamate-γ-semialdehyde. When the amino group of PMP is transferred to the α-KG, it forms glutamate and regenerates PLP.

The protein Ornithine Aminotransferase (OAT), in humans (hOAT), is an enzyme that catalyzes the the transfer of an amino group from L-ornithine(L-Orn) to α-ketoglutarate (α-KG). Its ligand, pyridoxal-5'-phosphate (<scene name='93/934004/Plp/1'>PLP</scene>), is a cofactor of this reaction. An amino group from L-Orn is transferred to PLP which converts it to pyridoxamine phosphate (PMP) and L-Orn is converted to L-glutamate-γ-semialdehyde. When the amino group of PMP is transferred to the α-KG, it forms glutamate and regenerates PLP.

== Biological relevance and broader implications ==

hOAT is found in most tissues in the body but predominates in the liver and kidney. There is a need to study the enzyme hOAT because the overexpression of this protein aids the proliferation of cancer cells, specifically Hepatocellular carcinoma (HCC), a common form of liver cancer. hOAT has been a target for mechanism-based inactivators (MBIs) in ongoing drug design efforts. HCC is normally diagnosed at advanced stages where the tumors tend to be resistant to radiotherapy and chemotherapy, making this type of cancer difficult to treat.

Sandbox Reserved 1760: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 6: / Line 6: @@
 == Function of your protein ==
-The protein Ornithine Aminotransferase (OAT), in humans (hOAT), is an enzyme that catalyzes the the transfer of an amino group from L-ornithine(L-Orn) to α-ketoglutarate (α-KG). Its ligand, pyridoxal-5'-phosphate (PLP), is a cofactor of this reaction. An amino group from L-Orn is transferred to PLP which converts it to pyridoxamine phosphate (PMP) and L-Orn is converted to L-glutamate-γ-semialdehyde. When the amino group of PMP is transferred to the α-KG, it forms glutamate and regenerates PLP.
+The protein Ornithine Aminotransferase (OAT), in humans (hOAT), is an enzyme that catalyzes the the transfer of an amino group from L-ornithine(L-Orn) to α-ketoglutarate (α-KG). Its ligand, pyridoxal-5'-phosphate (<scene name='93/934004/Plp/1'>PLP</scene>), is a cofactor of this reaction. An amino group from L-Orn is transferred to PLP which converts it to pyridoxamine phosphate (PMP) and L-Orn is converted to L-glutamate-γ-semialdehyde. When the amino group of PMP is transferred to the α-KG, it forms glutamate and regenerates PLP.
 == Biological relevance and broader implications ==
 hOAT is found in most tissues in the body but predominates in the liver and kidney. There is a need to study the enzyme hOAT because the overexpression of this protein aids the proliferation of cancer cells, specifically Hepatocellular carcinoma (HCC), a common form of liver cancer. hOAT has been a target for mechanism-based inactivators (MBIs) in ongoing drug design efforts. HCC is normally diagnosed at advanced stages where the tumors tend to be resistant to radiotherapy and chemotherapy, making this type of cancer difficult to treat.