The N-terminal sequence after residue 247 plays an important role in structure and function of Lon protease from Brevibacillus thermoruber WR-249

Biochemical and Biophysical Research Communications

Volumn 382, Issue 4, 2009, Pages 762-765

  Chir, Jiun Ly ^a   Liao, Jiahn Haur ^a   Lin, Yu Ching ^b   Wu, Shih Hsiung ^a,b  

^a INSTITUTE OF BIOLOGICAL CHEMISTRY   (Taiwan)

^b NATIONAL TAIWAN UNIVERSITY   (Taiwan)

Author keywords

ATP dependent protease; Brevibacillus thermoruber; Gel filtration chromatography; Lon protease

Indexed keywords

ADENOSINE TRIPHOSPHATASE; AMINO ACID; ENDOPEPTIDASE LA; PEPTIDASE; PROTEINASE;

AMINO TERMINAL SEQUENCE; ARTICLE; BREVIBACILLUS; BREVIBACILLUS THERMORUBER; ENZYME ACTIVITY; ENZYME STRUCTURE; MUTANT; NONHUMAN; PRIORITY JOURNAL; PROTEIN QUATERNARY STRUCTURE; STRUCTURE ACTIVITY RELATION;

ADENOSINE TRIPHOSPHATASES; AMINO ACID SEQUENCE; BACILLUS; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; PEPTIDE HYDROLASES; PROTEASE LA; PROTEIN STRUCTURE, TERTIARY; STRUCTURE-ACTIVITY RELATIONSHIP;

BREVIBACILLUS THERMORUBER;

EID: 64549123881     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.03.109     Document Type: Article

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