Structural and functional analysis of PUR2,5 gene encoding bifunctional enzyme of de novo purine biosynthesis in Ogataea (Hansenula) polymorpha CBS 4732T.

We describe the cloning, sequencing and functional characterization of gene PUR2,5, involved in de novo purine biosynthesis of the yeast Ogataea (Hansenula) polymorpha. This gene (2369 bp) was cloned by genetic complementation of adenine requiring mutation. It encodes a bifunctional enzyme of 789 amino acids (85 kDa) that catalyzes the second and the fifth steps of de novo purine biosynthesis pathway and shows dual enzymatic activity - of glycinamide ribotide synthetase (GARS, EC 6.

Myroides guanonis sp. nov., isolated from prehistoric paintings.

A novel psychrotolerant, strictly aerobic, non-motile, rod-shaped bacterial strain, designated IM13(T), was isolated from a sample taken from prehistoric guano paintings in Magura Cave, northwest Bulgaria and subjected to a polyphasic taxonomic study. Strain IM13(T) formed yellow colonies on LB agar plates and was Gram-staining-negative, heterotrophic and alkalitolerant. It grew optimally at pH 7.

Isolation and identification of alpha,alpha-trehalose and glycerol from an arctic psychrotolerant Streptomyces sp. SB9 and their possible role in the strain's survival.

Streptomyces sp. strain SB9 was isolated from perm frost soil samples in Spitsbergen, Arctic Ocean; it grows in a temperature range between 4 degrees C and 28 degrees C. During the survey of biologically active metabolites biosynthesized by this strain, significant amounts of alpha,alpha-trehalose (1) and glycerol (2) were detected.