Purification and Properties of API–2b→API–2c Converting Protease from<i>Streptomyces griseoincarnatus</i>Strain No. KTo–250, an API–2 Producer

Uyeda, Masaru; Suzuki, Keitarou; Sugiyama, Mieko; Shibata, Motoo

doi:10.1080/00021369.1979.10863723

Cited by 4 publications

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“…Humanserum-inter a (I),24) one of the Kunitz inhibitors has methionine residue as reactive amino acid. But, generally there are many "methionine" inhibitors among the Kazal inhibitors such as Korai pheasant ovomucoid 3,25) duck ovomucoid 3,24) Japanese quail ovoinhibitor domain 524) and so on. With respect to the reactive site, Met-Ile, API-2 is identical with Japanese quail ovoinhibitor domain 5.…”

Section: Carboxypeptidase Adigestion Ofpeptidementioning

confidence: 99%

Studies on alkaline protease inhibitor (API-2) produced by Streptomyces griseoincarnatus strain No. KTo-250. Part VII. Partial amino acid sequence of an alkaline protease inhibitor, API-2 (b and c).

Suzuki

Uyeda

Shibata

1981

Agricultural and Biological Chemistry

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API-2b and API-2c (alkaline protease inhibitors)were directly subjected to Edman degradation. It was elucidated that API-2c was lacking in Ala-Pro-Ser-Leu-Gly-Ala located in the NH2-terminal region of API-2b, so the two inhibitors were heterogeneous in the NH2-terminal region. Cleavage of the three methionyl bonds in API-2c with cyanogen bromide resulted in three fragments, designated as Peptide 1, Peptide 2 and Peptide 3. It was found that Peptide 1 was located at the NH2-terminal region, Peptide 2 was in the center and Peptide 3 made-up the COOH-terminal region of the API-2 molecule. Partial sequence data showed that most threonine, alanine, glycine and leucine residues were distributed in the NH2-terminal half of the molecule, and the rest of the molecule contained most of the aromatic residues. The amino acid sequence around the reactive site ofAPI-2 (b and c) was very similar to that of S-SI (Streptomyces subtilisin inhibitor) with the exception of the isoleucine residue in place of valine residue in S-SI.

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Section: Carboxypeptidase Adigestion Ofpeptidementioning

confidence: 99%

Studies on alkaline protease inhibitor (API-2) produced by Streptomyces griseoincarnatus strain No. KTo-250. Part VII. Partial amino acid sequence of an alkaline protease inhibitor, API-2 (b and c).

Suzuki

Uyeda

Shibata

1981

Agricultural and Biological Chemistry

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“…API-2c lacks the NH2-terminal six amino acid residues of API-2b, so they are heterogeneous in NH2-terminal region. As described in the previous paper, 3 ) the conversion of API-2b to API-2c was performed by an API-2b~API-2c converting protease produced by S. griseoincarnatus strain No. KTo-250, the producer of API-2b and API-2c.…”

Section: Partial Amino Acid Sequence Of Api-2 (Band C)mentioning

confidence: 99%

Partial Amino Acid Sequence of an Alkaline Protease Inhibitor, API-2 (b and c)

Suzuki

Uyeda

Shibata

1981

Agricultural and Biological Chemistry

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“…Purification procedures and some properties of API-2b and API-2c have also been described. The strain produced API-2b , API-2c converting protease 3 ) and API-2 degrading protease 4 ) which were thought to be concerned in the fate of API-2 in the growing system. Purification procedures and some properties of these enzymes have also been described.…”

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confidence: 99%

Formation and Dissociation of Complex between Alkaline Protease Inhibitor (API-2c) and Subtilisin BPN′

Suzuki¹,

Uyeda²,

Shibata³

1980

Agricultural and Biological Chemistry

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Purification and Properties of API–2b→API–2c Converting Protease fromStreptomyces griseoincarnatusStrain No. KTo–250, an API–2 Producer

Cited by 4 publications

References 0 publications

Studies on alkaline protease inhibitor (API-2) produced by Streptomyces griseoincarnatus strain No. KTo-250. Part VII. Partial amino acid sequence of an alkaline protease inhibitor, API-2 (b and c).

Studies on alkaline protease inhibitor (API-2) produced by Streptomyces griseoincarnatus strain No. KTo-250. Part VII. Partial amino acid sequence of an alkaline protease inhibitor, API-2 (b and c).

Partial Amino Acid Sequence of an Alkaline Protease Inhibitor, API-2 (b and c)

Formation and Dissociation of Complex between Alkaline Protease Inhibitor (API-2c) and Subtilisin BPN′

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