グルタミルアミノペプチダーゼ
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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2016/03/02 12:43:09」(JST)
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glutamyl aminopeptidase (aminopeptidase A) |
Identifiers |
Symbol |
ENPEP |
Alt. symbols |
gp160, CD249 |
Entrez |
2028 |
HUGO |
3355 |
OMIM |
138297 |
RefSeq |
NM_001977 |
UniProt |
Q07075 |
Other data |
EC number |
3.4.11.7 |
Locus |
Chr. 4 q25 |
Glutamyl aminopeptidase (EC 3.4.11.7, aminopeptidase A, aspartate aminopeptidase, angiotensinase A, glutamyl peptidase, Ca2+-activated glutamate aminopeptidase, membrane aminopeptidase II, antigen BP-1/6C3 of mouse B lymphocytes, L-aspartate aminopeptidase, angiotensinase A2) is an enzyme encoded by the ENPEP gene. Glutamyl aminopeptidase has also recently been designated CD249 (cluster of differentiation 249).
Glutamyl aminopeptidase is a zinc-dependent membrane-bound aminopeptidase that catalyzes the cleavage of glutamatic and aspartatic amino acid residues from the N-terminus of polypeptides. The enzyme degrades vasoconstricting angiotensin II into angiotensin III and therefore helps to regulate blood pressure.[1]
References
- ^ Reaux A, Iturrioz X, Vazeux G, Fournie-Zaluski MC, David C, Roques BP, Corvol P, Llorens-Cortes C (2000). "Aminopeptidase A, which generates one of the main effector peptides of the brain renin-angiotensin system, angiotensin III, has a key role in central control of arterial blood pressure". Biochem. Soc. Trans. 28 (4): 435–40. doi:10.1042/0300-5127:0280435. PMID 10961935.
External links
- The MEROPS online database for peptidases and their inhibitors: M01.003
- Glutamyl aminopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
Hydrolase: proteases (EC 3.4)
|
|
3.4.11-19: Exopeptidase |
3.4.11 |
- Aminopeptidase
- Alanine
- Arginyl
- Aspartyl
- Cystinyl
- Leucyl
- Glutamyl
- Methionyl
- O
|
|
3.4.13 |
|
|
3.4.14 |
- Dipeptidyl peptidase
- Cathepsin C
- Dipeptidyl peptidase-4
- Tripeptidyl peptidase
- Tripeptidyl peptidase I
- Tripeptidyl peptidase II
|
|
3.4.15 |
- Angiotensin-converting enzyme
|
|
3.4.16 |
- Serine type carboxypeptidases: Cathepsin A
- DD-transpeptidase
|
|
3.4.17 |
- Metalloexopeptidases
- Carboxypeptidase
- A
- A2
- B
- C
- E
- Glutamate II
|
|
Other/ungrouped |
|
|
|
3.4.21-25: Endopeptidase |
- Serine protease
- Cysteine protease
- Aspartic acid protease
- Metalloendopeptidase
- Threonine endopeptidase
- Proteasome endopeptidase complex
- HslU—HslV peptidase
- Other/ungrouped: Amyloid precursor protein secretase
- Alpha secretase
- Beta-secretase 1
- Beta-secretase 2
- Gamma secretase
|
|
3.4.99: Unknown |
|
|
UpToDate Contents
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English Journal
- Simple purification method for a recombinantly expressed native His-tag-free aminopeptidase A from Lactobacillus delbrueckii.
- Stressler T1, Tanzer C2, Ewert J2, Claaßen W2, Fischer L2.
- Protein expression and purification.Protein Expr Purif.2016 Nov 1;131:7-15. doi: 10.1016/j.pep.2016.10.010. [Epub ahead of print]
- The aminopeptidase A (PepA; EC 3.4.11.7) is an intracellular exopeptidase present in lactic acid bacteria. The PepA cleaves glutamyl/aspartyl residues from the N-terminal end of peptides and can, therefore, be applied for the production of protein hydrolysates with an increased amount of these amino
- PMID 27815133
- [Clinical features of different clinical forms of childhood congenital hepatic fibrosis].
- Wu X1, DU XR, Ding JF, Wu MJ, Luo SQ, Feng XZ.
- Zhongguo dang dai er ke za zhi = Chinese journal of contemporary pediatrics.Zhongguo Dang Dai Er Ke Za Zhi.2016 Apr;18(4):335-9.
- OBJECTIVE: To compare the clinical features of children with different clinical forms of congenital hepatic fibrosis (CHF), and provides a description of the characteristics of childhood CHF.METHODS: Sixty children with CHF between January 2002 and June 2015 were enrolled, including 26 children with
- PMID 27097579
- A Novel Glutamyl (Aspartyl)-Specific Aminopeptidase A from Lactobacillus delbrueckii with Promising Properties for Application.
- Stressler T1, Ewert J1, Merz M1, Funk J2, Claaßen W1, Lutz-Wahl S1, Schmidt H2, Kuhn A3, Fischer L1.
- PloS one.PLoS One.2016 Mar 22;11(3):e0152139. doi: 10.1371/journal.pone.0152139. eCollection 2016.
- Lactic acid bacteria (LAB) are auxotrophic for a number of amino acids. Thus, LAB have one of the strongest proteolytic systems to acquit their amino acid requirements. One of the intracellular exopeptidases present in LAB is the glutamyl (aspartyl) specific aminopeptidase (PepA; EC 3.4.11.7). Most
- PMID 27003449
Japanese Journal
- Purification and Characterization of an N-Terminal Acidic Amino Acid-Specific Aminopeptidase from Soybean Cotyledons (Glycine max)
- Bioscience, biotechnology, and biochemistry 74(1), 113-118, 2010-01-23
- NAID 10027550265
- 髄膜炎菌 Neisseria meningitidis の病原性に関する研究
Related Links
- Glutamyl aminopeptidase (EC:3.4.11.7) Short name: EAP Alternative name(s): Aminopeptidase A Short name: AP-A Differentiation antigen gp160 CD_antigen: CD249 Gene names i Name:ENPEP Organism i Homo sapiens i 9606 ...
- Gene ID: 2028, updated on 2-Oct-2016 Summary Other designations glutamyl aminopeptidase, AP-A, EAP, aminopeptidase A, differentiation antigen gp160, glutamyl aminopeptidase (aminopeptidase A) GeneRIFs: Gene References ...
★リンクテーブル★
[★]
- 英
- glutamyl aminopeptidase
[★]
アミノペプチダーゼ