Amino acid homologies between human biotinidase and bacterial aliphatic amidases: Putative identification of the active site of biotinidase

K. L. Swango, J. Hymes, P. Brown, B. Wolf*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

15 Scopus citations

Abstract

A search of protein databases revealed amino acid homologies among human biotinidase, bacterial aliphatic amidases, and bacterial and plant nitrilases. Amino acids YRK210-212 of biotinidase are conserved among the enzyme families. This homology and naturally occurring mutations that cause biotinidase deficiency suggest that this region is essential for enzyme activity land is conserved from bacteria. Cys245 is likely the cysteine in the active site of biotinidase. (C) 2000 Academic Press.

Original languageEnglish (US)
Pages (from-to)111-115
Number of pages5
JournalMolecular Genetics and Metabolism
Volume69
Issue number2
DOIs
StatePublished - Feb 2000

Keywords

  • Active site
  • Aliphatic amidase
  • Biotinidase
  • Nitrilase

ASJC Scopus subject areas

  • Endocrinology, Diabetes and Metabolism
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Endocrinology

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