Journal article
Biochemical Properties and Atomic Resolution Structure of a Proteolytically Processed β-Mannanase from Cellulolytic Streptomyces sp. SirexAA-E
Abstract
β-Mannanase SACTE_2347 from cellulolytic Streptomyces sp. SirexAA-E is abundantly secreted into the culture medium during growth on cellulosic materials. The enzyme is composed of domains from the glycoside hydrolase family 5 (GH5), fibronectin type-III (Fn3), and carbohydrate binding module family 2 (CBM2). After secretion, the enzyme is proteolyzed into three different, catalytically active variants with masses of 53, 42 and 34 kDa …
Authors
Takasuka TE; Acheson JF; Bianchetti CM; Prom BM; Bergeman LF; Book AJ; Currie CR; Fox BG
Journal
PLOS ONE, Vol. 9, No. 4,
Publisher
Public Library of Science (PLoS)
DOI
10.1371/journal.pone.0094166
ISSN
1932-6203