Cloning and sequencing of a gene for Mucor rennin, an aspartate protease from Mucor pusillus.
AUTOR(ES)
Tonouchi, N
RESUMO
The aspartate protease of Mucor pusillus (Mucor pusillus rennin; MPR) is a milk-clotting enzyme used in the cheese industry. The partial amino acid sequence of MPR was determined and oligonucleotide probes were synthesized for cloning of the MPR gene. A clone giving positive hybridization with the probes was selected from the cosmid library. Sequencing of the cloned DNA revealed an open reading frame of 1281 bp without introns which encodes 361 amino acids for the expected MPR with an NH2-terminal extension of 66 amino acids. MPR seems to be synthesized as a prepro enzyme.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=311780Documentos Relacionados
- Milk-clotting Enzyme from Microorganisms: V. Purification and Crystallization of Mucor Rennin from Mucor pusillus var. Lindt.1
- Purification and Properties of Mucor pusillus Acid Protease1
- Cloning and sequencing of Serratia protease gene.
- Toxicity of pymetrozine and thiamethoxam to Aphelinus gossypii and Delphastus pusillus.
- Conditions Influencing the Synthesis of Acid Protease by Mucor pusillus Lindt1