(Q27664390)

English

The N Domain of Human Angiotensin-I-converting Enzyme: THE ROLE OF N-GLYCOSYLATION AND THE CRYSTAL STRUCTURE IN COMPLEX WITH AN N DOMAIN-SPECIFIC PHOSPHINIC INHIBITOR, RXP407

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The N Domain of Human Angiotensin-I-converting Enzyme: THE ROLE OF N-GLYCOSYLATION AND THE CRYSTAL STRUCTURE IN COMPLEX WITH AN N DOMAIN-SPECIFIC PHOSPHINIC INHIBITOR, RXP407 (English)

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crystal structure

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author name string

Colin S Anthony

1

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Hazel R Corradi

2

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Sylva L U Schwager

3

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Pierre Redelinghuys

4

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Dimitris Georgiadis

5

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Vincent Dive

6

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K Ravi Acharya

7

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Edward D Sturrock

8

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publication date

12 November 2010

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Journal of Biological Chemistry

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285

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46

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35685-93

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Structure of testis ACE glycosylation mutants and evidence for conserved domain movement

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RXP 407, a phosphinic peptide, is a potent inhibitor of angiotensin I converting enzyme able to differentiate between its two active sites

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Identification of N-linked glycosylation sites in human testis angiotensin-converting enzyme and expression of an active deglycosylated form

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Different glycosylation requirements for the synthesis of enzymatically active angiotensin-converting enzyme in mammalian cells and yeast

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Naturally occurring active N-domain of human angiotensin I-converting enzyme

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Novel anti-inflammatory mechanisms of N-Acetyl-Ser-Asp-Lys-Pro in hypertension-induced target organ damage.

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Identifiers

10.1074/JBC.M110.167866

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