PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 6816278-8 1982 Aminooxyacetate, an inhibitor of alanine aminotransferase, completely inhibited this efflux and glandular pyruvate production. Pyruvic Acid 106-114 glutamic--pyruvic transaminase Homo sapiens 33-57 18584649-8 1988 A route for the biosynthesis of L-alanine that does not incorporate the enzyme alanine aminotransferase was revealed by MPS during synthesis of alternative pathways which produce L-alanine from pyruvate. Pyruvic Acid 194-202 glutamic--pyruvic transaminase Homo sapiens 79-103 529550-0 1979 Human red cell GPT polymorphism: comparison of the activities among different phenotypes using pyruvate and L-glutamate as substrates. Pyruvic Acid 95-103 glutamic--pyruvic transaminase Homo sapiens 15-18 32110376-4 2020 The blood glutamate scavengers, oxaloacetate and pyruvate, degrade glutamate in the blood to its inactive metabolite, 2-ketoglutarate, by the coenzymes glutamate-oxaloacetate transaminase (GOT) and glutamate-pyruvate transaminase (GPT), respectively. Pyruvic Acid 49-57 glutamic--pyruvic transaminase Homo sapiens 198-229 849292-1 1977 Data are provided which indicate that pyruvate and/or acetaldehyde can reverse the inhibition of alanine aminotransferase and aspartate aminotransferase by amino-oxyacetate. Pyruvic Acid 38-46 glutamic--pyruvic transaminase Homo sapiens 97-121 32110376-4 2020 The blood glutamate scavengers, oxaloacetate and pyruvate, degrade glutamate in the blood to its inactive metabolite, 2-ketoglutarate, by the coenzymes glutamate-oxaloacetate transaminase (GOT) and glutamate-pyruvate transaminase (GPT), respectively. Pyruvic Acid 49-57 glutamic--pyruvic transaminase Homo sapiens 231-234 28521864-1 2017 OBJECTIVES: Hepatic glutamic pyruvic transaminase (GPT; also known as alanine aminotransferase) is a gluconeogenesis enzyme that catalyzes conversions between alanine and pyruvic acid. Pyruvic Acid 171-183 glutamic--pyruvic transaminase Homo sapiens 51-54 31533027-7 2019 Mechanistically, this vulnerability reflects the low expression of alanine aminotransferase, the enzyme required for interconverting pyruvate and alanine, whereas activated T cells instead induce alanine transporters. Pyruvic Acid 133-141 glutamic--pyruvic transaminase Homo sapiens 67-91 28521864-1 2017 OBJECTIVES: Hepatic glutamic pyruvic transaminase (GPT; also known as alanine aminotransferase) is a gluconeogenesis enzyme that catalyzes conversions between alanine and pyruvic acid. Pyruvic Acid 171-183 glutamic--pyruvic transaminase Homo sapiens 70-94 19360321-4 2009 Here, we show that ALT1 and 2 possess similar enzymatic activity for alanine and pyruvate but with different Km and kcat values, while recombinant ALT2_2 protein does not possess any enzymatic activity. Pyruvic Acid 81-89 glutamic--pyruvic transaminase Homo sapiens 19-29 27258319-7 2016 We propose a model showing (i) how pyruvate derived from active glycolysis upon hypoxia is competitively used by the alanine aminotransferase/glutamate synthase cycle, leading to alanine accumulation and NAD+ regeneration. Pyruvic Acid 35-43 glutamic--pyruvic transaminase Homo sapiens 117-141 27258319-10 2016 Pyruvate produced by the reverse reaction of alanine aminotransferase is funneled to the TCA cycle, while deaminating glutamate dehydrogenase regenerates, reducing equivalent (NADH) and 2-oxoglutarate to maintain the cycle function. Pyruvic Acid 0-8 glutamic--pyruvic transaminase Homo sapiens 45-69 20641814-6 2004 In the cytoplasm, Pyr is converted into alanine (Ala) by glutamine-Pyr transaminase (GPT) and reversibly oxidized back to Lac by lactate dehydrogenase (LDH). Pyruvic Acid 18-21 glutamic--pyruvic transaminase Homo sapiens 85-88 12834898-2 2003 Glutamate pyruvate transaminase (GPT) is a highly active glutamate degrading enzyme that requires pyruvate as a co-substrate. Pyruvic Acid 10-18 glutamic--pyruvic transaminase Homo sapiens 33-36 12766182-2 2003 We hypothesized that 5 days of STT would attenuate pyruvate production and the increase in muscle tricarboxylic acid cycle intermediates (TCAI) during exercise, because of reduced flux through the reaction catalyzed by alanine aminotransferase (AAT; pyruvate + glutamate <--> 2-oxoglutarate + alanine). Pyruvic Acid 250-258 glutamic--pyruvic transaminase Homo sapiens 219-243 12834898-12 2003 In the setting of incubation with this large load of glutamate, neuroprotection by GPT was enhanced by adding pyruvate to the medium. Pyruvic Acid 110-118 glutamic--pyruvic transaminase Homo sapiens 83-86 11986392-1 2002 We tested the hypotheses that: (i) exercise with low muscle glycogen would reduce pyruvate flux through the alanine aminotransferase (AAT) reaction and attenuate the increase in tricarboxylic acid (TCA) cycle intermediates, and (ii) attenuation of tricarboxylic acid cycle intermediate (TCAI) pool expansion would limit TCA cycle flux, thereby accelerating phosphocreatine (PCr) degradation. Pyruvic Acid 82-90 glutamic--pyruvic transaminase Homo sapiens 108-132 11863375-1 2002 Alanine aminotransferase (ALT) catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate, and thereby has a key role in the intermediary metabolism of glucose and amino acids. Pyruvic Acid 114-122 glutamic--pyruvic transaminase Homo sapiens 0-24 7602770-1 1995 Alanine aminotransferase (Alt, L-alanine:2-oxoglutalate aminotransferase) is a pyridoxal enzyme which catalyses the reversible interconversion of L-alanine and 2-oxoglutalate to pyruvate and L-glutamate. Pyruvic Acid 178-186 glutamic--pyruvic transaminase Homo sapiens 0-24 11746419-4 2001 L-cycloserine, an inhibitor of alanine aminotransferase, inhibited glutamate synthesis less than 15% when added in the presence of 5 mM pyruvate but 47% in the presence of 0.2 mM pyruvate. Pyruvic Acid 136-144 glutamic--pyruvic transaminase Homo sapiens 31-55 11746419-4 2001 L-cycloserine, an inhibitor of alanine aminotransferase, inhibited glutamate synthesis less than 15% when added in the presence of 5 mM pyruvate but 47% in the presence of 0.2 mM pyruvate. Pyruvic Acid 179-187 glutamic--pyruvic transaminase Homo sapiens 31-55 11255139-3 2001 Glutamate appears to be a key substrate for the rapid increase in muscle TCA cycle intermediates (TCAI) that occurs at the onset of moderate to intense exercise, due to a rightward shift of the reaction catalyzed by alanine aminotransferase (glutamate + pyruvate <==> alanine + 2-oxoglutarate). Pyruvic Acid 254-262 glutamic--pyruvic transaminase Homo sapiens 216-240 2205108-7 1990 In conclusion 1) loss of 3H relative to 14C from position 6 in glucose occurs during lactate formation in extrahepatic tissues possibly due to the GPT reaction (alanine conversion to pyruvate), and 2) even under supraphysiologic hyperinsulinemic conditions not all of plasma lactate originates from plasma glucose. Pyruvic Acid 183-191 glutamic--pyruvic transaminase Homo sapiens 147-150