AI Article Synopsis
- Researchers cloned the structural gene for GTP-cyclohydrolase, crucial for riboflavin production, from a Pichia guilliermondii genomic library.
- They isolated and sequenced a 1855 bp DNA fragment that corrected riboflavin deficiency in mutant strains of E. coli and P. guilliermondii.
- The enzyme encoded is predicted to be 344 amino acids long, closely related to similar enzymes in E. coli, Baccillus subtilis, and Saccharomyces cerevisiae, and likely functions as a tetramer.
Article Abstract
The structural gene of GTP-cyclohydrolase, involved in riboflavin biosynthesis, was cloned from a Pichia guilliermondii genomic library. A 1855 bp genomic DNA fragment complementing the riboflavin auxotrophies of an Escherichia coli ribA mutant, defective in GTP-cyclohydrolase II, and a P. guilliermondii rib1 mutant was isolated and sequenced. An open reading frame with the potential to encode a protein of 344 amino acids with a predicted molecular mass of 38,711 Da was detected. The P. guilliermondii enzyme shows a high degree of homology to GTP-cyclohydrolases type II from E. coli and Baccillus subtilis and to GTP-cyclohydrolase from Saccharomyces cerevisiae. Functional GTP-cyclohydrolase from P. guilliermondii may consist of four identical subunits.
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| http://dx.doi.org/10.1002/yea.320111005 | DOI Listing |
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