PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 18922879-2 2009 In the present study, structurally diverse coenzyme-substrate derivatives mimicking this type for pyridoxal 5"-phosphate-dependent human ornithine decarboxylase (hODC), a potential anticancer target, were designed, synthesized, and tested to elucidate the structural requirements for optimal inhibition of intracellular ODC as well as of tumor cell proliferation. Pyridoxal Phosphate 98-120 ornithine decarboxylase 1 Homo sapiens 137-160 20406645-8 2010 Phytomonas ODC required pyridoxal 5"-phosphate for maximum activity and was specifically inhibited by alpha-difluoromethylornithine. Pyridoxal Phosphate 24-46 ornithine decarboxylase 1 Homo sapiens 11-14 24524072-4 2014 The active form of vitamin B6, pyridoxal 5-phosphate, is, besides its antioxidative properties, a cofactor for a variety of essential enzymes present in the malaria parasite which includes the ornithine decarboxylase (ODC, synthesis of polyamines), the aspartate aminotransferase (AspAT, involved in the protein biosynthesis), and the serine hydroxymethyltransferase (SHMT, a key enzyme within the folate metabolism). Pyridoxal Phosphate 31-52 ornithine decarboxylase 1 Homo sapiens 193-216 24524072-4 2014 The active form of vitamin B6, pyridoxal 5-phosphate, is, besides its antioxidative properties, a cofactor for a variety of essential enzymes present in the malaria parasite which includes the ornithine decarboxylase (ODC, synthesis of polyamines), the aspartate aminotransferase (AspAT, involved in the protein biosynthesis), and the serine hydroxymethyltransferase (SHMT, a key enzyme within the folate metabolism). Pyridoxal Phosphate 31-52 ornithine decarboxylase 1 Homo sapiens 218-221 21640851-1 2011 Diaminopimelate decarboxylase (DAPDC) and ornithine decarboxylase (ODC) are pyridoxal 5"-phosphate dependent enzymes that are critical to microbial growth and pathogenicity. Pyridoxal Phosphate 76-98 ornithine decarboxylase 1 Homo sapiens 42-65 21640851-1 2011 Diaminopimelate decarboxylase (DAPDC) and ornithine decarboxylase (ODC) are pyridoxal 5"-phosphate dependent enzymes that are critical to microbial growth and pathogenicity. Pyridoxal Phosphate 76-98 ornithine decarboxylase 1 Homo sapiens 67-70 18922879-2 2009 In the present study, structurally diverse coenzyme-substrate derivatives mimicking this type for pyridoxal 5"-phosphate-dependent human ornithine decarboxylase (hODC), a potential anticancer target, were designed, synthesized, and tested to elucidate the structural requirements for optimal inhibition of intracellular ODC as well as of tumor cell proliferation. Pyridoxal Phosphate 98-120 ornithine decarboxylase 1 Homo sapiens 162-166 18922879-2 2009 In the present study, structurally diverse coenzyme-substrate derivatives mimicking this type for pyridoxal 5"-phosphate-dependent human ornithine decarboxylase (hODC), a potential anticancer target, were designed, synthesized, and tested to elucidate the structural requirements for optimal inhibition of intracellular ODC as well as of tumor cell proliferation. Pyridoxal Phosphate 98-120 ornithine decarboxylase 1 Homo sapiens 163-166 9605314-7 1998 The key residues that interact directly with pyridoxal-P were identical in ornithine decarboxylase and the two GADs, thus allowing us to make a specific structural prediction of the cofactor binding site of GAD. Pyridoxal Phosphate 45-56 ornithine decarboxylase 1 Homo sapiens 75-98 12460114-2 2002 To inhibit pyridoxal-5"-phosphate dependent ornithine decarboxylase and pyruvate dependent S-adenosylmethionine decarboxylase, key enzymes of polyamine biosynthesis, a system of substrate-like O-substituted hydroxylamines is suggested. Pyridoxal Phosphate 11-33 ornithine decarboxylase 1 Homo sapiens 44-67 10222205-5 1999 GAD65 has structural similarities to ornithine decarboxylase in the pyridoxal-5"-phosphate-binding middle domain (residues 201-460) and to dialkylglycine decarboxylase in the C-terminal domain (residues 461-585). Pyridoxal Phosphate 68-90 ornithine decarboxylase 1 Homo sapiens 37-60 34560100-2 2021 The polyamines putrescine, agmatine and cadaverine, are produced by pyridoxal 5"-phosphate-dependent L-ornithine, L-arginine and L-lysine decarboxylases (ODC, ADC, LDC), respectively, from both the alanine racemase (AR) and aspartate aminotransferase (AAT) folds. Pyridoxal Phosphate 68-90 ornithine decarboxylase 1 Homo sapiens 154-157 7670372-4 1995 Through the analysis of known barrel structures we developed a topographic model of the pyridoxal phosphate-binding domain of ornithine decarboxylase, which predicts that the Schiff base lysine and a conserved glycine-rich sequence both map to the C-termini of the beta-strands. Pyridoxal Phosphate 88-107 ornithine decarboxylase 1 Homo sapiens 126-149 34796899-4 2021 A previous crystal structure of an ODC-APA complex indicated that APA non-covalently binds ODC and its cofactor pyridoxal 5-phosphate (PLP) and functions by competing with the ODC substrate ornithine for binding to the catalytic site. Pyridoxal Phosphate 112-133 ornithine decarboxylase 1 Homo sapiens 35-38 34796899-4 2021 A previous crystal structure of an ODC-APA complex indicated that APA non-covalently binds ODC and its cofactor pyridoxal 5-phosphate (PLP) and functions by competing with the ODC substrate ornithine for binding to the catalytic site. Pyridoxal Phosphate 112-133 ornithine decarboxylase 1 Homo sapiens 91-94 34796899-4 2021 A previous crystal structure of an ODC-APA complex indicated that APA non-covalently binds ODC and its cofactor pyridoxal 5-phosphate (PLP) and functions by competing with the ODC substrate ornithine for binding to the catalytic site. Pyridoxal Phosphate 135-138 ornithine decarboxylase 1 Homo sapiens 35-38 34796899-4 2021 A previous crystal structure of an ODC-APA complex indicated that APA non-covalently binds ODC and its cofactor pyridoxal 5-phosphate (PLP) and functions by competing with the ODC substrate ornithine for binding to the catalytic site. Pyridoxal Phosphate 135-138 ornithine decarboxylase 1 Homo sapiens 91-94 901421-5 1977 Ornithine decarboxylase activity was decreased by vitamin B-6 deficiency when assayed in tissue extracts without addition of pyridoxal phosphate, but was greater than in control extracts when pyridoxal phosphate was present in saturating amounts. Pyridoxal Phosphate 125-144 ornithine decarboxylase 1 Homo sapiens 0-23 901421-5 1977 Ornithine decarboxylase activity was decreased by vitamin B-6 deficiency when assayed in tissue extracts without addition of pyridoxal phosphate, but was greater than in control extracts when pyridoxal phosphate was present in saturating amounts. Pyridoxal Phosphate 192-211 ornithine decarboxylase 1 Homo sapiens 0-23