Primary structure of an inactive mutant of phospholipase A2 in the venom of Bungarus fasciatus (banded krait).
From the acidic components of Bungarus fasciatus venom, a very small amount (0.16%) of a novel phospholipase A2 was obtained. Both neurotoxicity and enzyme activity were found to be lacking. Amino acid sequence study showed that it has a normal backbone of group I snake venom phospholipase A2 with 118 amino acid residues. The lack of enzyme activity was attributed to its mutation of the indispensable Asp residue to an Ala residue, i.e., the usual His-Asp47 turned out to be His-Ala47. This is the eighth isoform of phospholipase A2 found from the venom of Bungarus fasciatus. Examination of structural homology with three other isoforms revealed 66% similarity at most.
Liu
C S
CS
Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan, Republic of China.
Kuo
P Y
PY
Chen
J M
JM
Chen
S W
SW
Chang
C H
CH
Tseng
C C
CC
Tzeng
M C
MC
Lo
T B
TB
D000595:Amino Acid Sequence; D002038:Bungarotoxins / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification; D002853:Chromatography, Liquid; D008969:Molecular Sequence Data; D009154:Mutation; D010741:Phospholipases A / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification; D054467:Phospholipases A2; D017386:Sequence Homology, Amino Acid
D002038:Bungarotoxins; D010741:Phospholipases A; D054467:Phospholipases A2