Literature summary for 3.4.11.22 extracted from

Goto, Y.; Ogawa, K.; Nakamura, T.J.; Hattori, A.; Tsujimoto, M.
Substrate-dependent nitric oxide synthesis by secreted endoplasmic reticulum aminopeptidase 1 in macrophages (2015), J. Biochem., 157, 439-449.

Search for more literature for 3.4.11.22

Cloned(Commentary)

Cloned (Comment)	Organism
expression in RAW264.7 cell	Mus musculus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
105000	-	x * 105000, SDS-PAGE	Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	Q9EQH2	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining

Subunits

Subunits	Comment	Organism
?	x * 105000, SDS-PAGE	Mus musculus

Synonyms

Synonyms	Comment	Organism
ERAP1	-	Mus musculus

General Information

General Information	Comment	Organism
physiological function	in the presence of aminopeptidase inhibitor amastatin, nitric oxide synthesis in activated RAW264.7 cells is significantly decreased. Subsequently, significant reduction of nitric oxide synthesis is observed in aminopeptidase ERAP1 knockdown cells compared with wild-type cells. This reduction is rescued by exogenously added ERAP1. When peritoneal macrophages prepared from ERAP1 knockout mouse are employed, reduction of nitric oxide synthesis in knockout mouse macrophages is also attributable to ERAP1. In the presence of amastatin, further reduction is observed in knockout mouse-derived macrophages	Mus musculus

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)