PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 20174634-6 2010 CONCLUSIONS/SIGNIFICANCE: Our structural data suggest that a deletion of three amino acids in E. coli SSADH permits this enzyme to use NADP+, whereas in contrast the human enzyme utilises NAD+. NAD 188-192 aldehyde dehydrogenase 5 family member A1 Homo sapiens 102-107 18588919-5 2008 This recombinant cattle tick protein has potent NAD(+)-dependent SSADH activity, but possesses also marked enzymatic activity on other aliphatic and aromatic aldehyde substrates. NAD 48-54 aldehyde dehydrogenase 5 family member A1 Homo sapiens 65-70 33203024-3 2020 Here, we present a patient with a severe phenotype of SSADHD caused by a novel genetic variant c.728T > C that leads to an exchange of leucine to proline at residue 243, located within the highly conserved nicotinamide adenine dinucleotide (NAD)+ binding domain of SSADH. NAD 206-239 aldehyde dehydrogenase 5 family member A1 Homo sapiens 54-59 33203024-3 2020 Here, we present a patient with a severe phenotype of SSADHD caused by a novel genetic variant c.728T > C that leads to an exchange of leucine to proline at residue 243, located within the highly conserved nicotinamide adenine dinucleotide (NAD)+ binding domain of SSADH. NAD 241-244 aldehyde dehydrogenase 5 family member A1 Homo sapiens 54-59