Sequence and structure of the rat housekeeping PBG-D isoform
Porphobilinogen deaminase (PBG-D), a key enzyme in the tetrapyrrole biosynthetic pathway, is encoded by a single gene containing two different promoters. The upstream promoter, found in all cell types, initiates the transcription of the housekeeping PBG-D isoform, whereas the downstream one is eryth...
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_0006291X_v249_n2_p438_Cardalda |
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todo:paper_0006291X_v249_n2_p438_Cardalda2023-10-03T14:03:46Z Sequence and structure of the rat housekeeping PBG-D isoform Cardalda, C.A. Batlle, A. Juknat, A.A. complementary DNA isoenzyme porphobilinogen deaminase amino acid sequence animal tissue article enzyme active site enzyme glycosylation enzyme phosphorylation enzyme structure exon housekeeping gene male myristylation nonhuman nucleotide sequence priority journal protein secondary structure rat sequence homology Animalia Rodentia Porphobilinogen deaminase (PBG-D), a key enzyme in the tetrapyrrole biosynthetic pathway, is encoded by a single gene containing two different promoters. The upstream promoter, found in all cell types, initiates the transcription of the housekeeping PBG-D isoform, whereas the downstream one is erythroid-specific. In this study, we provide the first full sequence of a 1086 bp cDNA covering the coding region for the rat ubiquitous PBG-D and its primary amino acid sequence. The cDNA encodes a 39,361 Da protein composed of 361 amino acids. Nucleotide sequence comparison between both isoforms from rat shows similarities of 99.5%, with four changes (C/G) in exon 8 and only one (C/A) in exon 12. Secondary structure prediction reveals that 76.5% of the amino acids from exon 1 are located in a loop. Potential phosphorylation, glycosylation, and myristoylation sites were revealed through motif searches. Housekeeping PBG-D contains coiled-coil segments known to be involved in dynamic rearrangements in the active site. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_0006291X_v249_n2_p438_Cardalda |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
complementary DNA isoenzyme porphobilinogen deaminase amino acid sequence animal tissue article enzyme active site enzyme glycosylation enzyme phosphorylation enzyme structure exon housekeeping gene male myristylation nonhuman nucleotide sequence priority journal protein secondary structure rat sequence homology Animalia Rodentia |
| spellingShingle |
complementary DNA isoenzyme porphobilinogen deaminase amino acid sequence animal tissue article enzyme active site enzyme glycosylation enzyme phosphorylation enzyme structure exon housekeeping gene male myristylation nonhuman nucleotide sequence priority journal protein secondary structure rat sequence homology Animalia Rodentia Cardalda, C.A. Batlle, A. Juknat, A.A. Sequence and structure of the rat housekeeping PBG-D isoform |
| topic_facet |
complementary DNA isoenzyme porphobilinogen deaminase amino acid sequence animal tissue article enzyme active site enzyme glycosylation enzyme phosphorylation enzyme structure exon housekeeping gene male myristylation nonhuman nucleotide sequence priority journal protein secondary structure rat sequence homology Animalia Rodentia |
| description |
Porphobilinogen deaminase (PBG-D), a key enzyme in the tetrapyrrole biosynthetic pathway, is encoded by a single gene containing two different promoters. The upstream promoter, found in all cell types, initiates the transcription of the housekeeping PBG-D isoform, whereas the downstream one is erythroid-specific. In this study, we provide the first full sequence of a 1086 bp cDNA covering the coding region for the rat ubiquitous PBG-D and its primary amino acid sequence. The cDNA encodes a 39,361 Da protein composed of 361 amino acids. Nucleotide sequence comparison between both isoforms from rat shows similarities of 99.5%, with four changes (C/G) in exon 8 and only one (C/A) in exon 12. Secondary structure prediction reveals that 76.5% of the amino acids from exon 1 are located in a loop. Potential phosphorylation, glycosylation, and myristoylation sites were revealed through motif searches. Housekeeping PBG-D contains coiled-coil segments known to be involved in dynamic rearrangements in the active site. |
| format |
JOUR |
| author |
Cardalda, C.A. Batlle, A. Juknat, A.A. |
| author_facet |
Cardalda, C.A. Batlle, A. Juknat, A.A. |
| author_sort |
Cardalda, C.A. |
| title |
Sequence and structure of the rat housekeeping PBG-D isoform |
| title_short |
Sequence and structure of the rat housekeeping PBG-D isoform |
| title_full |
Sequence and structure of the rat housekeeping PBG-D isoform |
| title_fullStr |
Sequence and structure of the rat housekeeping PBG-D isoform |
| title_full_unstemmed |
Sequence and structure of the rat housekeeping PBG-D isoform |
| title_sort |
sequence and structure of the rat housekeeping pbg-d isoform |
| url |
http://hdl.handle.net/20.500.12110/paper_0006291X_v249_n2_p438_Cardalda |
| work_keys_str_mv |
AT cardaldaca sequenceandstructureoftherathousekeepingpbgdisoform AT batllea sequenceandstructureoftherathousekeepingpbgdisoform AT juknataa sequenceandstructureoftherathousekeepingpbgdisoform |
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1782030414648442880 |