Purification and Characterization of Dipeptidyl Aminopeptidase from<i>Aureobacterium</i>sp. WO26

Ogasawara, Wataru; Inanobe, Noriyuki; Ochiai, Keiko; Ando, Katsuhiko; Okada, Hirofumi; Morikawa, Yasushi

doi:10.1271/bbb.61.146

Cited by 2 publications

(2 citation statements)

References 7 publications

(9 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…DPP II (EC 3.4.14.2), a serine protease with an acidic optimum pH of 4.5-6, preferentially cleaves dipeptides from the N-termini of X-ala-or X-pro-NA. DPP III (EC 3.4.14.4) is a serine protease with an optimum pH of [8][9][10].…”

Section: Introductionmentioning

confidence: 99%

“…DPP IV (EC 3.4.14.5), a serine protease with an optimum pH of 8-9, specifically cleaves gly-pro from the N-termini of its substrates. Several DPPs, including some with specificities different from those in mammals, have recently been identified in microorganisms (2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12) including Dictyostelium discoideum (13)(14)(15)(16).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Purification and characterization of a novel dipeptidyl peptidase from Dictyostelium discoideum

Choi

Jones

1999

IUBMB Life

View full text Add to dashboard Cite

SUMMARY:A dipeptidyl peptidase (DPP) was purified to homogeneity using lys-ala-J~-naphthylamide, the standard substrate for DPP I1. The enzyme is a monomer with a Mr of 70kDa, pl 5.2, and Km 5.0t1M. Its terminal amino acid sequence was XXLLYA|QKRLF and was not identical to that of any known protein. Although initially considered to be a DPP II, the enzyme differed in some properties from classical DPP IIs. It had a pH optimum of 7.9, was not active on X-pro-naphthylamides, the usual substrates of mammalian DPP II, but was active on arg-arg-and asp-arg-naphthylamides, substrates acted on by the DPP III class of enzymes. This enzyme therefore combines properties typical of both DPP II and I11 and differs from all previously described DPPs. Activity on lys-ala-[~-naphthylamide was most abundant during aggregation and its activity is consistent with processing specific peptides during development.

show abstract

Section: Introductionmentioning

confidence: 99%