PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 1631127-3 1992 Insertion mutants in ahcY lack detectable S-adenosyl-L-homocysteine hydrolase activity and, as a consequence, S-adenosyl-L-homocysteine accumulates in the cells, resulting in a 16-fold decrease in the intracellular ratio of S-adenosyl-L-methionine to S-adenosyl-L-homocysteine as compared to wild-type cells. S-Adenosylmethionine 224-247 adenosylhomocysteinase Homo sapiens 21-25 21528287-4 1997 Treatment of human ovarian cancer cells 2008 and the cisplatin-resistant subline 2008/C13*5.25 with the S-adenosylhomocysteine hydrolase inhibitor adenosine-dialdehyde, an indirect inhibitor of transmethylation, resulted in a significant elevation (16-fold in 2008, 6-fold in 2008/C13*5.25) in the cellular content of S-adenosylhomocysteine without changing S-adenosylmethionine. S-Adenosylmethionine 358-378 adenosylhomocysteinase Homo sapiens 104-136 11607550-1 1995 S-Adenosylhomocysteine hydrolase (SAHH) is a key enzyme in transmethylation reactions that use S-adenosylmethionine as the methyl donor. S-Adenosylmethionine 95-115 adenosylhomocysteinase Homo sapiens 0-32 11607550-1 1995 S-Adenosylhomocysteine hydrolase (SAHH) is a key enzyme in transmethylation reactions that use S-adenosylmethionine as the methyl donor. S-Adenosylmethionine 95-115 adenosylhomocysteinase Homo sapiens 34-38 18769049-1 2008 BACKGROUND/AIMS: S-Adenosylhomocysteine hydrolase (AdoHcyase) catalyzes the reversible hydrolysis of S-adenosylhomocysteine (AdoHcy), which is a potent product inhibitor of S-adenosylmethionine (AdoMet)-dependent methyltransferases. S-Adenosylmethionine 173-193 adenosylhomocysteinase Homo sapiens 17-49 18769049-1 2008 BACKGROUND/AIMS: S-Adenosylhomocysteine hydrolase (AdoHcyase) catalyzes the reversible hydrolysis of S-adenosylhomocysteine (AdoHcy), which is a potent product inhibitor of S-adenosylmethionine (AdoMet)-dependent methyltransferases. S-Adenosylmethionine 173-193 adenosylhomocysteinase Homo sapiens 51-60 18769049-1 2008 BACKGROUND/AIMS: S-Adenosylhomocysteine hydrolase (AdoHcyase) catalyzes the reversible hydrolysis of S-adenosylhomocysteine (AdoHcy), which is a potent product inhibitor of S-adenosylmethionine (AdoMet)-dependent methyltransferases. S-Adenosylmethionine 195-201 adenosylhomocysteinase Homo sapiens 17-49 18769049-1 2008 BACKGROUND/AIMS: S-Adenosylhomocysteine hydrolase (AdoHcyase) catalyzes the reversible hydrolysis of S-adenosylhomocysteine (AdoHcy), which is a potent product inhibitor of S-adenosylmethionine (AdoMet)-dependent methyltransferases. S-Adenosylmethionine 195-201 adenosylhomocysteinase Homo sapiens 51-60 12910461-1 2003 S-adenosylhomocysteine hydrolase (SAHH) is a key regulator of S-adenosylmethionine-dependent methylation reactions and an interesting pharmacologic target. S-Adenosylmethionine 64-82 adenosylhomocysteinase Homo sapiens 34-38 1631127-5 1992 The ahcY mutant, when grown in supplemented medium, synthesizes significantly reduced levels of bacteriochlorophyll, indicating that modulation of the intracellular ratio of S-adenosyl-L-methionine to S-adenosyl-L-homocysteine may be an important factor in regulating bacteriochlorophyll biosynthesis. S-Adenosylmethionine 174-197 adenosylhomocysteinase Homo sapiens 4-8 2260986-4 1990 The above data are consistent with the metabolism of SAM to ATP by a route recently identified by us whereby ATP is formed from deoxyadenosine: namely binding to the enzyme S-adenosylhomocysteine hydrolase with subsequent release of adenine and further conversion to ATP via APRT. S-Adenosylmethionine 53-56 adenosylhomocysteinase Homo sapiens 173-205 33993848-7 2022 Our study uncovers a new axis of SAH-AHCYL1-PIK3C3, which senses the intracellular level of SAH to inhibit autophagy in an MTORC1-independent manner.Abbreviations: ADOX: adenosine dialdehyde; AHCY: adenosylhomocysteinase; AHCYL1: adenosylhomocysteinase like 1; cLEU: cycloleucine; PIK3C3: phosphatidylinositol 3-kinase catalytic subunit type 3; PtdIns3P: phosphatidylinositol-3-phosphate; SAH: S-adenosyl-l-homocysteine; SAM: S-adenosyl-l-methionine. S-Adenosylmethionine 426-449 adenosylhomocysteinase Homo sapiens 37-41 34647332-8 2022 LINC00662 can reduce the promoter methylation level of s-adenosylmethionine (SAM)-dependent hepatocellular carcinoma (HCC)-promoting genes by regulating the MAT1A/SAM and AHCY/SAH axes, thereby promoting the activation of oncogenes. S-Adenosylmethionine 55-75 adenosylhomocysteinase Homo sapiens 171-175 34647332-8 2022 LINC00662 can reduce the promoter methylation level of s-adenosylmethionine (SAM)-dependent hepatocellular carcinoma (HCC)-promoting genes by regulating the MAT1A/SAM and AHCY/SAH axes, thereby promoting the activation of oncogenes. S-Adenosylmethionine 77-80 adenosylhomocysteinase Homo sapiens 171-175 6254019-2 1980 dAdo also inactivates the enzyme S-adenosylhomocysteine hydrolase (AdoHcyase; S-adenosyl-L-homocystein hydrolase EC 3.3.1.1) which is involved in the catabolism of S-adenosyl-L-homocysteine (AdoHcy), both a product and a potent inhibitor of S-adenosylmethionine-dependent transmethylation. S-Adenosylmethionine 241-261 adenosylhomocysteinase Homo sapiens 33-65 6254019-2 1980 dAdo also inactivates the enzyme S-adenosylhomocysteine hydrolase (AdoHcyase; S-adenosyl-L-homocystein hydrolase EC 3.3.1.1) which is involved in the catabolism of S-adenosyl-L-homocysteine (AdoHcy), both a product and a potent inhibitor of S-adenosylmethionine-dependent transmethylation. S-Adenosylmethionine 241-261 adenosylhomocysteinase Homo sapiens 67-76 31959915-8 2020 In addition, we demonstrated that some SAM-dependent HCC-promoting genes could be regulated by LINC00662 by altering the methylation status of their promoters via the LINC00662-coupled axes of MAT1A/SAM and AHCY/SAH. S-Adenosylmethionine 39-42 adenosylhomocysteinase Homo sapiens 207-211 33328229-4 2020 SAH is a potent feedback inhibitor of S-adenosylmethionine (SAM)-dependent methyltransferases, and timely hydrolysis of SAH by AHCY is critical to sustain methylation reactions. S-Adenosylmethionine 38-58 adenosylhomocysteinase Homo sapiens 127-131 33328229-4 2020 SAH is a potent feedback inhibitor of S-adenosylmethionine (SAM)-dependent methyltransferases, and timely hydrolysis of SAH by AHCY is critical to sustain methylation reactions. S-Adenosylmethionine 60-63 adenosylhomocysteinase Homo sapiens 127-131 31959915-7 2020 Mechanistically, LINC00662 was determined to regulate the key enzymes influencing SAM and SAH levels, namely, methionine adenosyltransferase 1A (MAT1A) and S-adenosylhomocysteine hydrolase (AHCY), by RNA-RNA and RNA-protein interactions. S-Adenosylmethionine 82-85 adenosylhomocysteinase Homo sapiens 156-188 31959915-7 2020 Mechanistically, LINC00662 was determined to regulate the key enzymes influencing SAM and SAH levels, namely, methionine adenosyltransferase 1A (MAT1A) and S-adenosylhomocysteine hydrolase (AHCY), by RNA-RNA and RNA-protein interactions. S-Adenosylmethionine 82-85 adenosylhomocysteinase Homo sapiens 190-194 33035507-1 2020 3-Deazadenosine (3-DA) is a general methylation inhibitor that depletes S-adenosylmethionine, a methyl donor, by blocking S-adenosylhomocysteine hydrolase (SAHH). S-Adenosylmethionine 72-92 adenosylhomocysteinase Homo sapiens 122-154 33035507-1 2020 3-Deazadenosine (3-DA) is a general methylation inhibitor that depletes S-adenosylmethionine, a methyl donor, by blocking S-adenosylhomocysteine hydrolase (SAHH). S-Adenosylmethionine 72-92 adenosylhomocysteinase Homo sapiens 156-160 31959915-8 2020 In addition, we demonstrated that some SAM-dependent HCC-promoting genes could be regulated by LINC00662 by altering the methylation status of their promoters via the LINC00662-coupled axes of MAT1A/SAM and AHCY/SAH. S-Adenosylmethionine 199-202 adenosylhomocysteinase Homo sapiens 207-211 18815415-1 2008 S-adenosylhomocysteine hydrolase (SAHH) is a ubiquitous enzyme that plays a central role in methylation-based processes by maintaining the intracellular balance between S-adenosylhomocysteine (SAH) and S-adenosylmethionine. S-Adenosylmethionine 202-222 adenosylhomocysteinase Homo sapiens 34-38 26527160-7 2015 An asymptomatic 7-year old son of the proband is also homozygous for the AHCY-R49H mutation and has elevated serum aminotransferase levels, as well as markedly elevated serum levels of SAH, S-adenosylmethionine (SAM), and methionine, which are hallmarks of SAH hydrolase deficiency. S-Adenosylmethionine 190-210 adenosylhomocysteinase Homo sapiens 73-77 26527160-7 2015 An asymptomatic 7-year old son of the proband is also homozygous for the AHCY-R49H mutation and has elevated serum aminotransferase levels, as well as markedly elevated serum levels of SAH, S-adenosylmethionine (SAM), and methionine, which are hallmarks of SAH hydrolase deficiency. S-Adenosylmethionine 212-215 adenosylhomocysteinase Homo sapiens 73-77 27678102-5 2017 We postulate that alterations in the micronutrient metabolism may affect the regulation of enzymes, methionine adenosyltransferase ( MAT2A), and SAH-hydrolase ( AHCY), involved in the production of methyl donor S-adenosylmethionine (SAM), thereby influencing the methylation potential (MP) in the placenta of women delivering preterm. S-Adenosylmethionine 211-231 adenosylhomocysteinase Homo sapiens 161-165 27678102-5 2017 We postulate that alterations in the micronutrient metabolism may affect the regulation of enzymes, methionine adenosyltransferase ( MAT2A), and SAH-hydrolase ( AHCY), involved in the production of methyl donor S-adenosylmethionine (SAM), thereby influencing the methylation potential (MP) in the placenta of women delivering preterm. S-Adenosylmethionine 233-236 adenosylhomocysteinase Homo sapiens 161-165 23079506-2 2013 In mammals, the rate-limiting step of the S-adenosylmethionine-dependent methylation process is exclusively controlled by S-adenosylhomocysteine (S-AdoHcy) hydrolase (SAHH). S-Adenosylmethionine 44-62 adenosylhomocysteinase Homo sapiens 167-171 19201949-3 2009 Reduced Ahcy activity in dtp mutants led to elevated levels of S-adenosylhomocysteine (SAH) and, to a lesser degree, of its metabolic precursor S-adenosylmethionine (SAM). S-Adenosylmethionine 144-164 adenosylhomocysteinase Homo sapiens 8-12 19201949-3 2009 Reduced Ahcy activity in dtp mutants led to elevated levels of S-adenosylhomocysteine (SAH) and, to a lesser degree, of its metabolic precursor S-adenosylmethionine (SAM). S-Adenosylmethionine 166-169 adenosylhomocysteinase Homo sapiens 8-12