RGD Reference Report - Probing the active site of rat porphobilinogen synthase using newly developed inhibitors. - Rat Genome Database

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Probing the active site of rat porphobilinogen synthase using newly developed inhibitors.

Authors: Li, N  Chu, X  Liu, X  Li, D 
Citation: Li N, etal., Bioorg Chem. 2009 Feb;37(1):33-40. Epub 2008 Dec 17.
RGD ID: 4144201
Pubmed: PMID:19095280   (View Abstract at PubMed)
DOI: DOI:10.1016/j.bioorg.2008.11.001   (Journal Full-text)

The structurally related tetrapyrrolic pigments are a group of natural products that participate in many of the fundamental biosynthetic and catabolic processes of living organisms. Porphobilinogen synthase catalyzes a rate-limiting step for the biosyntheses of tetrapyrrolic natural products. In the present study, a variety of new substrate analogs and reaction intermediate analogs were synthesized, which were used as probes for studying the active site of rat porphobilinogen synthase. The compounds 1, 3, 6, 9, 14, 16, and 28 were found to be competitive inhibitors of rat porphobilinogen synthase with inhibition constants ranging from 0.96 to 73.04mM. Compounds 7, 10, 12, 13, 15, 17, 18, and 26 were found to be irreversible enzyme inhibitors. For irreversible inhibitors, loose-binding inhibitors were found to give stronger inactivation. The amino group and carboxyl group of the analogs were found to be important for their binding to the enzyme. This study increased our understanding of the active site of porphobilinogen synthase.



Gene Ontology Annotations    Click to see Annotation Detail View

Molecular Function

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
AladRatporphobilinogen synthase activity  IDA  RGD 

Objects Annotated

Genes (Rattus norvegicus)
Alad  (aminolevulinate dehydratase)


Additional Information