Characterization of an Extracellular Dipeptidase from Streptococcus gordonii FSS2
2005 ◽
Vol 73
(2)
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pp. 1256-1259
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Keyword(s):
Its Gene
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ABSTRACT PepV, a dipeptidase found in culture fluids of Streptococcus gordonii FSS2, was purified and characterized, and its gene was cloned. PepV is a monomeric metalloenzyme of approximately 55 kDa that preferentially degrades hydrophobic dipeptides. The gene encodes a polypeptide of 467 amino acids, with a theoretical molecular mass of 51,114 Da and a calculated pI of 4.8. The S. gordonii PepV gene is homologous to the PepV gene family from Lactobacillus and Lactococcus spp.
1998 ◽
Vol 11
(5)
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pp. 429-433
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Keyword(s):
2000 ◽
Vol 20
(18)
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pp. 6935-6944
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Keyword(s):
Genome-wide Characterization of Major Intrinsic Protein (MIP) Gene Family in Brachypodium distachyon
2018 ◽
Vol 13
(5)
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pp. 536-552
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Keyword(s):
1992 ◽
Vol 66
(12)
◽
pp. 7389-7396
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Keyword(s):