Crystallization and preliminary X-ray investigation of proteinase A, a non-pepsin-type acid proteinase from Aspergillus niger var. macrosporus

Tanokura, Masaru; Matsuzaki, Hidemi; Iwata, So; Nakagawa, Atsushi; Hamaya, Toru; Takizawa, Toshio; Takahashi, Kenji

doi:10.1016/0022-2836(92)90738-6

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Aspergilloglutamic Peptidase and Its Homologs1

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Cited by 10 publications

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“…We obtained three kinds of the enzyme crystals (types I, II and III) under different conditions. 180,181) Type I contained one molecule, and types II and III each contained two molecules of the monomeric enzyme per asymmetric unit. The type I enzyme was solved to a resolution of 1.4 Å (Fig.…”

Section: Aspergilloglutamic Peptidase and Its Homologsmentioning

confidence: 99%

Structure and function studies on enzymes with a catalytic carboxyl group(s): from ribonuclease T<sub>1</sub> to carboxyl peptidases

Takahashi

2013

Proceedings of the Japan Academy. Ser. B: Physical and Biologic

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A group of enzymes, mostly hydrolases or certain transferases, utilize one or a few side-chain carboxyl groups of Asp and/or Glu as part of the catalytic machinery at their active sites. This review follows mainly the trail of studies performed by the author and his colleagues on the structure and function of such enzymes, starting from ribonuclease T1, then extending to three major types of carboxyl peptidases including aspartic peptidases, glutamic peptidases and serine-carboxyl peptidases.

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Section: Aspergilloglutamic Peptidase and Its Homologsmentioning

confidence: 99%