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Title: Biochemical and Structural Characterization of a Ureidoglycine Aminotransferase in the Klebsiella pneumoniae Uric Acid Catabolic Pathway

Many plants, fungi, and bacteria catabolize allantoin as a mechanism for nitrogen assimilation. Recent reports have shown that in plants and some bacteria the product of hydrolysis of allantoin by allantoinase is the unstable intermediate ureidoglycine. While this molecule can spontaneously decay, genetic analysis of some bacterial genomes indicates that an aminotransferase may be present in the pathway. Here we present evidence that Klebsiella pneumoniae HpxJ is an aminotransferase that preferentially converts ureidoglycine and an {alpha}-keto acid into oxalurate and the corresponding amino acid. We determined the crystal structure of HpxJ, allowing us to present an explanation for substrate specificity.
Authors:
;  [1]
  1. (Cornell)
Publication Date:
OSTI Identifier:
1002658
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemistry-US; Journal Volume: 49; Journal Issue: (29) ; 07, 2010
Research Org:
Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
Sponsoring Org:
USDOE
Country of Publication:
United States
Language:
ENGLISH
Subject:
36 MATERIALS SCIENCE; ALLANTOIN; AMINO ACIDS; AMINOTRANSFERASES; BACTERIA; CRYSTAL STRUCTURE; DECAY; FUNGI; GENETICS; HYDROLYSIS; KLEBSIELLA; NITROGEN; SPECIFICITY; SUBSTRATES; URIC ACID