Guojun Zheng

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A novel (+)-γ-lactamase used for the resolution of racemic γ-lactam from Bradyrhizobium japonicum USDA 6 was found as a result of sequence-structure guided genome mining. It consists of 409 amino acids, only 49% of which are identical to the amino acid sequences of the known (+)-γ-lactamase from Sulfolobus solfataricus. This is only the third(More)
The formation of inclusion bodies (IBs) in recombinant protein biotechnology has become one of the most frequent undesirable occurrences in both research and industrial applications. So far, the pET System is the most powerful system developed for the production of recombinant proteins when Escherichia coli is used as the microbial cell factory. Also, using(More)
A thermostable formamidase from the hyperthermophilic archaeon Sulfolobus solfataricus P2 was revealed to be a novel, thermostable (+)-γ-lactamase. This (+)-γ-lactamase (Sso2810) is composed of only 318 amino acid residues, in contrast to a previously reported (+)-γ-lactamase (Sso2122) with 504 amino acid residues from the same strain. Herein, we(More)
A thermostable formamidase from the aerobic hyperthermophilic archaeon Aeropyrum pernix was revealed a novel type II (+)-γ-lactamase. This type II (+)-γ-lactamase is only composed of 377 amino acid residues, in contrast to another thermostable (+)-γ-lactamase from Sulfolobus solfataricus with 504 amino acid residues (type I). It is interesting that there(More)
The enantiomers of 2-azabicyclo[2.2.1]hept-5-en-3-one (γ-lactam) are key chiral synthons in the synthesis of antiviral drugs such as carbovir and abacavir. (+)-γ-Lactamase can be used as a catalyst in the enzymatic preparation of optically pure (-)-γ-lactam. Here, a (+)-γ-lactamase discovered from Bradyrhizobium japonicum USDA 6 by sequence-structure guided(More)
Biocatalyzed synthesis of nucleoside analogues was carried out using two thermostable nucleoside phosphorylases from the hyperthermophilic aerobic crenarchaeon Aeropyrum pernix K1. The synthesis of the 2,6-diaminopurine nucleoside and 5-methyluridine was used as a reaction model to test the process. Both the purine nucleoside phosphorylase (apPNP) and(More)
An esterase, Sso2518, from Sulfolobus solfataricus P2 was over-expressed in E. coli. and characterized after purification. The maximum activity was at pH 7.5 and 50 degrees C. The half life of Sso2518 was about 30 min at 85 degrees C and the enzyme was activated by Cu(2+). The catalytic triad of Sso2518 was comprised of residues Ser151, Asp176, and His328.(More)
Using immobilized cells of a novel strain of Microbacterium hydrocarbonoxydans L29-9 in polymers of polyvinyl alcohol (PVA)-alginate-boric acid, enantioselective resolution of racemic γ-lactam to produce (-)γ-lactam was successfully carried out. A 6:1 ratio of PVA:sodium alginate not only prevented agglomeration of the matrix but also produced beads with(More)
Whole cells of Bradyrhizobium japonicum USDA 6 showed both (+)-γ-lactamase activity and (-)-γ-lactamase activity. Insight into the genome of B. japonicum USDA 6 revealed two potential γ-lactamases: a type I (+)-γ-lactamase and a (-)-γ-lactamase, making it the first strain to contain two totally different enantioselective lactamases. Both recombinant enzymes(More)
2-Azabicyclo[2.2.1]hept-5-en-3-one (γ-lactam) is an important precursor of many carbocyclic nucleoside analogs and pharmaceuticals. (−)-γ-Lactam has attracted much attention because of its role as an intermediate of antiviral drugs such as abacavir and carbovir. (+)-γ-Lactamase can be used for the kinetic resolution of γ-lactam to obtain (−)-γ-lactam. In(More)