Gilkes N R, Henrissat B, Kilburn D G, Miller R C, Warren R A
Department of Microbiology, University of British Columbia, Vancouver, Canada.
Microbiol Rev. 1991 Jun;55(2):303-15. doi: 10.1128/mr.55.2.303-315.1991.
Several types of domain occur in beta-1, 4-glycanases. The best characterized of these are the catalytic domains and the cellulose-binding domains. The domains may be joined by linker sequences rich in proline or hydroxyamino acids or both. Some of the enzymes contain repeated sequences up to 150 amino acids in length. The enzymes can be grouped into families on the basis of sequence similarities between the catalytic domains. There are sequence similarities between the cellulose-binding domains, of which two types have been identified, and also between some domains of unknown function. The beta-1, 4-glycanases appear to have arisen by the shuffling of a relatively small number of progenitor sequences.
β-1,4-聚糖酶中存在几种类型的结构域。其中特征最明确的是催化结构域和纤维素结合结构域。这些结构域可能由富含脯氨酸或羟基氨基酸或两者的连接序列相连。一些酶含有长度达150个氨基酸的重复序列。根据催化结构域之间的序列相似性，这些酶可分为不同的家族。纤维素结合结构域之间存在序列相似性，已鉴定出两种类型，并且在一些功能未知的结构域之间也存在序列相似性。β-1,4-聚糖酶似乎是由相对较少数量的祖源序列重排产生的。
