Macluralisin--a serine proteinase from fruits of Maclura pomifera (Raf.) Schneid.
A serine proteinase was isolated from fruits of Maclura pomifera (Raf.) Schneid. by affinity chromatography on bacitracin-containing sorbents and gel-filtration. The enzyme, named macluralisin, is a glycoprotein with a molecular mass of 65 kDa; its protein moiety corresponds to a molecular mass of 50 kDa. The substrate specificity of macluralisin towards synthetic peptides and insulin B-chain is similar to that of cucumisin, a subtilisin-like proteinase from melon fruit. The enzyme is completely inhibited by diisopropylfluorophosphate. Its amino-acid composition resembles that of a serine proteinase isolated from the Cucurbitaceae. The N-terminal sequence has 33% of its residues identical to those of the sequence of fungal subtilisin-like proteinase K. Hence, Maclura pomifera serine proteinase belongs to the subtilisin family, which seems to be broadly distributed in the plant kingdom.
Rudenskaya
G N
GN
Chemistry Department, Moscow State University, Russia.
Bogdanova
E A
EA
Revina
L P
LP
Golovkin
B N
BN
Stepanov
V M
VM
D000595:Amino Acid Sequence; D001414:Bacitracin; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D005638:Fruit / Q000201:enzymology*; D006023:Glycoproteins / Q000737:chemistry; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry / Q000302:isolation & purification*; D010944:Plants / Q000201:enzymology*; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000737:chemistry / Q000302:isolation & purification*; D013379:Substrate Specificity; D013381:Subtilisins / Q000737:chemistry / Q000302:isolation & purification*
D006023:Glycoproteins; D010940:Plant Proteins; D001414:Bacitracin; D012697:Serine Endopeptidases; D013381:Subtilisins; C093902:macluralisin