Substrate specificity of prorenin converting enzyme of mouse submandibular gland. Analysis using site-directed mutagenesis.

Nakayama, Kazuhisa; Kim, W S; Nakagawa, Tsutomu; Nagahama, Masami; Murakami, Kazuo

doi:10.1016/s0021-9258(17)45322-1

Cited by 15 publications

References 39 publications

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Renin

Morris¹

2000

Comprehensive Physiology

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The sections in this article are: The Renin Paper A blood pressure‐raising substance is formed in the kidneys and passed into the blood Time course of the pressure elevation following injection of renin Analysis of the mechanism underlying the pressure rise Renin Release Regulation Renin Gene: Structure and Control Background Renin Gene Structure Renin Promoter Structure Renin Promoter Control Transcription Factors Renin Messenger RNA Synthesis and Activation Biosynthesis of Prorenin Processing of Prorenin Structure of Renin Binding Protein(s) of Renin Genetic Studies Studies in Rats Studies in Humans Transgenic Mice and Rats Human Gene in Mice Renin Promoter–Simian Virus 40 T Antigen Transgenic Mice Human Promoter Transgenic Mice Ren‐2 Hypertensive Transgenic Rats Model of Malignant Hypertension Renin and Angiotensinogen Transgenic Mice and Rats Knockouts Summary and Challenges

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Renin

Morris¹

2000

Comprehensive Physiology

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The crystal structure of the mouse glandular kallikrein‐13 (prorenin converting enzyme)

Timm

1997

Protein Science

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A crystal structure of the serine protease, mouse glandular kallikrein 13 (mGK-13) has been determined at 2.6-A resolution. This enzyme, isolated from the mouse submandibular gland, is also known as prorenin-converting enzyme and cleaves submandibular gland Ren-2 prorenin to yield active renin. The mGK-13 structure is similar to other members of the mammalian serine protease family, having five conserved disulfide bonds and an active site located in the cleft between two P-barrel domains. The mGK-13 structure reveals for the first time an ordered kallikrein loop conformation containing a short 310 helix. This loop is disordered in the related porcine pancreatic kallikrein and rat submandibular tonin structures. The kallikrein loop is in close spatial proximity to the active site and is also involved in a dimeric arrangement of mGK-13. The catalytic specificity of mCK-13 for Ren-2 prorenin was studied by modeling a prorenin-derived peptide into the active site of mGK-13. This model emphasizes two electronegative substrate specificity pockets on the mGK-13 surface, which could accommodate the dibasic P2 and P1 residues at the site of prorenin cleavage by mGK-13.

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Kallikrein 13

2009

Class 3 Hydrolases

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Substrate specificity of prorenin converting enzyme of mouse submandibular gland. Analysis using site-directed mutagenesis.

Cited by 15 publications

References 39 publications

Renin

Renin

The crystal structure of the mouse glandular kallikrein‐13 (prorenin converting enzyme)

Kallikrein 13

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