Chandrasekaran, M; Jasmin, C; Sreeja, Chellappan; Sarita,G Bhat; Rajeev, Sukumaran K; Elyas, K K(Springer, January 10, 2010)
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Abstract:
An alkaline protease gene (Eap) was isolated
for the first time from a marine fungus, Engyodontium
album. Eap consists of an open reading frame of 1,161 bp
encoding a prepropeptide consisting of 387 amino acids
with a calculated molecular mass of 40.923 kDa. Homology
comparison of the deduced amino acid sequence of
Eap with other known proteins indicated that Eap encode
an extracellular protease that belongs to the subtilase
family of serine protease (Family S8). A comparative
homology model of the Engyodontium album protease
(EAP) was developed using the crystal structure of proteinase
K. The model revealed that EAP has broad substrate
specificity similar to Proteinase K with preference for
bulky hydrophobic residues at P1 and P4. Also, EAP is
suggested to have two disulfide bonds and more than two
Ca2? binding sites in its 3D structure; both of which are
assumed to contribute to the thermostable nature of the
protein.
Sarita,G Bhat; Jasmin, C; Sreeja, Chellappan; Rajeev, K Sukumaran; Elyas, K K; Chandrasekaran, M(Springer, January 10, 2010)
[+]
[-]
Abstract:
An alkaline protease gene (Eap) was isolated
for the first time from a marine fungus, Engyodontium
album. Eap consists of an open reading frame of 1,161 bp
encoding a prepropeptide consisting of 387 amino acids
with a calculated molecular mass of 40.923 kDa. Homology
comparison of the deduced amino acid sequence of
Eap with other known proteins indicated that Eap encode
an extracellular protease that belongs to the subtilase
family of serine protease (Family S8). A comparative
homology model of the Engyodontium album protease
(EAP) was developed using the crystal structure of proteinase
K. The model revealed that EAP has broad substrate
specificity similar to Proteinase K with preference for
bulky hydrophobic residues at P1 and P4. Also, EAP is
suggested to have two disulfide bonds and more than two
Ca2? binding sites in its 3D structure; both of which are
assumed to contribute to the thermostable nature of the
protein.
Description:
World J Microbiol Biotechnol (2010) 26:1269–1279
DOI 10.1007/s11274-009-0298-6