当前位置： SCI文献检索 > INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY期刊下所有文献 > An N-acetyllactosamine-specific lectin, PFA, isolated from a moth (Phalera flavescens), structurally resembles an invertebrate-type lysozyme.

An N-acetyllactosamine-specific lectin, PFA, isolated from a moth (Phalera flavescens), structurally resembles an invertebrate-type lysozyme.

Abstract：

:PFA (Phalera flavescens agglutinin) lectin purified from larvae of the lobster moth (P. flavescens) shows a strong binding ability specific to the N-acetyllactosamine (Galβ1-4GlcNAc) site. We determined the genomic and cDNA sequences of the PFA gene, which consists of five exons and spans approximately 5 kb of a genomic region. Surprisingly, the amino acid sequence (149 amino acids) was similar to invertebrate-type lysozymes and related proteins. The predicted tertiary structure of the PFA protein was similar to the lysozymes of clams such as the common orient clam (Meretrix lusoria) and Japanese littleneck (Venerupis philippinarum (Tapes japonica)). The PFA, however, lacks a catalytically essential amino acid, an Asp (D), which is one of the two important amino acids (Glu (E) and D) express the function of lysozyme. As a result, lysozyme activity assays indicated that PFA does not have lysozyme activity. Results suggest that the PFA gene evolved from a lysozyme gene through the loss of lysozyme activity sites and the acquisition of lectin activity during evolution of the genus Phalera.

journal_name

Insect Biochem Mol Biol

journal_title

Insect biochemistry and molecular biology

authors

Yokoyama K,Sato M,Haneda T,Yamazaki K,Kitano T,Umetsu K

doi

10.1016/j.ibmb.2014.09.005

subject

Has Abstract

pub_date

2014-11-01 00:00:00

pages

106-11

eissn

0965-1748

issn

1879-0240

pii

S0965-1748(14)00155-6

journal_volume

54

pub_type

杂志文章

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