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Cloning and sequencing of Serratia protease gene

Open access
Nakahama, Kazuo, Yoshimura, Koji, Marumoto, Ryuji, Kikuchi, Masakazu, Lee, In Sook, Hase, Toshiharu, Matsubara, Hiroshi·1986·Nucleic Acids Research

Abstract

The gene encoding an extracellular metalloproteinase from Serratia sp. E-15 has been cloned, and its complete nucleotide sequence determined. The amino acid sequence deduced from the nucleotide sequence reveals that the mature protein of the Serratia protease consists of 470 amino acids with a molecular weight of 50,632. The G+C content of the coding region for the mature protein is 58%; this high G+C content is due to a marked preference for G+C bases at the third position of the codons. The gene codes for a short pro-peptide preceding the mature protein. The Serratia protease gene was expressed in Escherichia coli and Serratia marcescens; the former produced the Serratia protease in the cells and the latter in the culture medium. Three zinc ligands and an active site of the Serratia protease were predicted by comparing the structure of the enzyme with those of thermolysin and Bacillus subtilis neutral protease.

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Metadata

Authors
Nakahama, K., Yoshimura, K., Marumoto, R., Kikuchi, M., Lee, I. S., Hase, T., & Matsubara, H.
Venue
Nucleic Acids Research
Published
1986
Volume
14
Issue
14
Pages
5843-5855
ISSN
  • 0305-1048 (ISSN-L)
  • 1362-4962
OpenAlex
W1987061077
Cited by
191
References
1
FWCI
5.66
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Cloning and sequencing of Serratia protease gene. https://app.cochat.ai/papers/10.1093/nar/14.14.5843
The paper
Nakahama, K., Yoshimura, K., Marumoto, R., Kikuchi, M., Lee, I. S., Hase, T., & Matsubara, H. (1986). Cloning and sequencing of Serratia protease gene. Nucleic Acids Research. https://doi.org/10.1093/nar/14.14.5843

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