Mapping a putative pyruvoyl decarboxylase active site to human cytomegalovirus open reading frame UL77.
Human cytomegalovirus is present as an apparently innocuous infection among a large proportion of the adult population that causes serious disease when congenitally transferred (1). Human cytomegalovirus disease may become life threatening when found as an infection of immunocompromised transplant and AIDS patients (1,2). We now map a putative pyruvoyl decarboxylase enzyme prosthetic group, known to be essential to the active site of this class of enzymes, to Human cytomegalovirus open reading frame UL77. The significance of finding a putative pyruvoyl decarboxylase enzyme prosthetic group among human cytomegalovirus open reading frame codons is p = 0.001. The UL77 polypeptide was aligned with human, yeast and bacterial S-AdoMet decarboxylase enzymes. Alignment of UL77 and S-AdoMet decarboxylase enzymes indicates that UL77 may contain a similar activity.
Microbiology Research Department, Kettering-Meyer Laboratory, Southern Research Institute, Birmingham, AL 35205.
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D012437:Adenosylmethionine Decarboxylase / Q000235:genetics; D000483:Alleles; D000595:Amino Acid Sequence; D001665:Binding Sites / Q000235:genetics*; D003587:Cytomegalovirus / Q000201:enzymology / Q000235:genetics*; D016208:Databases, Factual; D016679:Genome, Viral; D008969:Molecular Sequence Data; D016366:Open Reading Frames / Q000235:genetics; D011767:Pyruvate Decarboxylase / Q000235:genetics*; D016415:Sequence Alignment / Q000379:methods; D017386:Sequence Homology, Amino Acid; D012984:Software
D011767:Pyruvate Decarboxylase; D012437:Adenosylmethionine Decarboxylase