Nardilysin

NRDC
Identifiers
Aliases	NRDC, hNRD1, hNRD2, NRD1, nardilysin convertase, nardilysin
External IDs	OMIM: 602651; MGI: 1201386; GeneCards: NRDC
Enzyme activity
Gene location (Human)
Chr.	Chromosome 1 (human)
End	51,878,805 bp
Gene location (Mouse)
Chr.	Chromosome 4 (mouse)
End	108,918,974 bp
RNA expression pattern
	Top expressed in
	glutes; ; right testis; ; left testis; ; muscle of thigh; ; triceps brachii muscle; ; gastrocnemius muscle; ; anterior pituitary; ; sperm; ; Skeletal muscle tissue of biceps brachii; ; thoracic diaphragm;
	Top expressed in
	seminiferous tubule; ; tail of embryo; ; genital tubercle; ; granulocyte; ; spermatid; ; plantaris muscle; ; neural layer of retina; ; muscle of thigh; ; extensor digitorum longus muscle; ; lens;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	peptidase activity; protein binding; catalytic activity; metallopeptidase activity; hydrolase activity; metal ion binding; epidermal growth factor binding; metalloendopeptidase activity;
Cellular component	cell surface; cytosol; mitochondrion;
Biological process	positive regulation of membrane protein ectodomain proteolysis; cell population proliferation; neuromuscular junction development; cell migration; regulation of endopeptidase activity; proteolysis; negative regulation of cold-induced thermogenesis;
	Sources:Amigo / QuickGO
Orthologs
Databases	NCBI: entry; OMA: entry
	4898
	230598
	ENSG00000078618
	ENSMUSG00000053510
	O43847
	Q8BHG1
	NM_001101662; NM_001242361; NM_002525
	NM_146150; NM_001346554; NM_001347169
	NP_001095132; NP_001229290; NP_002516
	NP_001333483; NP_001334098; NP_666262
	Wikidata
View/Edit Human	View/Edit Mouse

Nardilysin (EC 3.4.24.61) is an enzyme that in humans is encoded by the gene NRDC (formally NRD1). Nardilysin is a type of protease, which means it functions to cut the bonds between certain amino acids. More specifically, it’s an endopeptidase that cleaves bonds at the N-terminus of arginine residues connected to other basic amino acids. This activity also explains its alternative name, N-arginine dibasic convertase, hence its standard name.

Interactions

Nardilysin has been shown to interact with Heparin-binding EGF-like growth factor.

Enzyme activity

Nardilysin is a type of enzyme also called N-arginine dibasic convertase or NRD-convertase. This enzyme catalyses the following chemical reaction:

Hydrolysis of polypeptides, preferably at -Xaa-Arg-Lys-, and less commonly at -Arg-Arg-Xaa-, in which Xaa is not Arg or Lys

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000078618 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000053510 – Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Hospital V, Prat A, Joulie C, Cherif D, Day R, Cohen P (May 1998). "Human and rat testis express two mRNA species encoding variants of NRD convertase, a metalloendopeptidase of the insulinase family". Biochem J. 327 (3): 773–9. doi:10.1042/bj3270773. PMC 1218856. PMID 9581555.
↑ Fumagalli P, Accarino M, Egeo A, Scartezzini P, Rappazzo G, Pizzuti A, Avvantaggiato V, Simeone A, Arrigo G, Zuffardi O, Ottolenghi S, Taramelli R (Apr 1998). "Human NRD convertase: a highly conserved metalloendopeptidase expressed at specific sites during development and in adult tissues". Genomics. 47 (2): 238–45. doi:10.1006/geno.1997.5078. PMID 9479496.
1 2 "Entrez Gene: NRD1 nardilysin (N-arginine dibasic convertase)".
↑ Nishi, E; Prat A; Hospital V; Elenius K; Klagsbrun M (Jul 2001). "N-arginine dibasic convertase is a specific receptor for heparin-binding EGF-like growth factor that mediates cell migration". EMBO J. 20 (13). England: 3342–50. doi:10.1093/emboj/20.13.3342. ISSN 0261-4189. PMC 125525. PMID 11432822.
↑ Gomez S, Gluschankof P, Morel A, Cohen P (September 1985). "The somatostatin-28 convertase of rat brain cortex is associated with secretory granule membranes". The Journal of Biological Chemistry. 260 (19): 10541–5. doi:10.1016/S0021-9258(19)85118-9. PMID 3897221.
↑ Gluschankof P, Gomez S, Morel A, Cohen P (July 1987). "Enzymes that process somatostatin precursors. A novel endoprotease that cleaves before the arginine-lysine doublet is involved in somatostatin-28 convertase activity of rat brain cortex". The Journal of Biological Chemistry. 262 (20): 9615–20. doi:10.1016/S0021-9258(18)47978-1. PMID 2885328.
↑ Chesneau V, Pierotti AR, Barré N, Créminon C, Tougard C, Cohen P (January 1994). "Isolation and characterization of a dibasic selective metalloendopeptidase from rat testes that cleaves at the amino terminus of arginine residues". The Journal of Biological Chemistry. 269 (3): 2056–61. doi:10.1016/S0021-9258(17)42134-X. PMID 8294457.
↑ Pierotti AR, Prat A, Chesneau V, Gaudoux F, Leseney AM, Foulon T, Cohen P (June 1994). "N-arginine dibasic convertase, a metalloendopeptidase as a prototype of a class of processing enzymes". Proceedings of the National Academy of Sciences of the United States of America. 91 (13): 6078–82. Bibcode:1994PNAS...91.6078P. doi:10.1073/pnas.91.13.6078. PMC 44141. PMID 8016118.

Seidah NG, Prat A (2003). "Precursor convertases in the secretory pathway, cytosol and extracellular milieu". Essays Biochem. 38: 79–94. doi:10.1042/bse0380079. PMID 12463163.
Hospital V, Prat A (2005). "Nardilysin, a basic residues specific metallopeptidase that mediates cell migration and proliferation". Protein Pept. Lett. 11 (5): 501–8. doi:10.2174/0929866043406508. PMID 15544571.
Winter AG, Pierotti AR (2001). "Gene expression of the dibasic-pair cleaving enzyme NRD convertase (N-arginine dibasic convertase) is differentially regulated in the GH3 pituitary and Mat-Lu prostate cell lines". Biochem. J. 351 (3): 755–64. doi:10.1042/0264-6021:3510755. PMC 1221416. PMID 11042131.
Nishi E, Prat A, Hospital V, et al. (2001). "N-arginine dibasic convertase is a specific receptor for heparin-binding EGF-like growth factor that mediates cell migration". EMBO J. 20 (13): 3342–50. doi:10.1093/emboj/20.13.3342. PMC 125525. PMID 11432822.
Ma Z, Csuhai E, Chow KM, Hersh LB (2001). "Expression of the acidic stretch of nardilysin as a functional binding domain". Biochemistry. 40 (31): 9447–52. doi:10.1021/bi010538x. PMID 11478915.
Hospital V, Nishi E, Klagsbrun M, et al. (2003). "The metalloendopeptidase nardilysin (NRDc) is potently inhibited by heparin-binding epidermal growth factor-like growth factor (HB-EGF)". Biochem. J. 367 (Pt 1): 229–38. doi:10.1042/BJ20020822. PMC 1222870. PMID 12095415.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Chow KM, Oakley O, Goodman J, et al. (2003). "Nardilysin cleaves peptides at monobasic sites". Biochemistry. 42 (7): 2239–44. doi:10.1021/bi027178d. PMID 12590613.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. Bibcode:2006Natur.441..315G. doi:10.1038/nature04727. PMID 16710414.
Nishi E, Hiraoka Y, Yoshida K, et al. (2006). "Nardilysin enhances ectodomain shedding of heparin-binding epidermal growth factor-like growth factor through activation of tumor necrosis factor-alpha-converting enzyme". J. Biol. Chem. 281 (41): 31164–72. doi:10.1074/jbc.M601316200. PMID 16923819.
Bernstein HG, Stricker R, Dobrowolny H, et al. (2007). "Histochemical evidence for wide expression of the metalloendopeptidase nardilysin in human brain neurons". Neuroscience. 146 (4): 1513–23. doi:10.1016/j.neuroscience.2007.02.057. PMID 17442499. S2CID 8060302.

This article on a gene on human chromosome 1 is a stub. You can help Wikipedia by adding missing information.

[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000078618 – Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000053510 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid9581555-5] Hospital V, Prat A, Joulie C, Cherif D, Day R, Cohen P (May 1998). "Human and rat testis express two mRNA species encoding variants of NRD convertase, a metalloendopeptidase of the insulinase family". Biochem J. 327 (3): 773–9. doi:10.1042/bj3270773. PMC 1218856. PMID 9581555.

[pmid9479496-6] Fumagalli P, Accarino M, Egeo A, Scartezzini P, Rappazzo G, Pizzuti A, Avvantaggiato V, Simeone A, Arrigo G, Zuffardi O, Ottolenghi S, Taramelli R (Apr 1998). "Human NRD convertase: a highly conserved metalloendopeptidase expressed at specific sites during development and in adult tissues". Genomics. 47 (2): 238–45. doi:10.1006/geno.1997.5078. PMID 9479496.

[entrez-7] 1 2 "Entrez Gene: NRD1 nardilysin (N-arginine dibasic convertase)".

[pmid11432822-8] Nishi, E; Prat A; Hospital V; Elenius K; Klagsbrun M (Jul 2001). "N-arginine dibasic convertase is a specific receptor for heparin-binding EGF-like growth factor that mediates cell migration". EMBO J. 20 (13). England: 3342–50. doi:10.1093/emboj/20.13.3342. ISSN 0261-4189. PMC 125525. PMID 11432822.

[9] Gomez S, Gluschankof P, Morel A, Cohen P (September 1985). "The somatostatin-28 convertase of rat brain cortex is associated with secretory granule membranes". The Journal of Biological Chemistry. 260 (19): 10541–5. doi:10.1016/S0021-9258(19)85118-9. PMID 3897221.

[10] Gluschankof P, Gomez S, Morel A, Cohen P (July 1987). "Enzymes that process somatostatin precursors. A novel endoprotease that cleaves before the arginine-lysine doublet is involved in somatostatin-28 convertase activity of rat brain cortex". The Journal of Biological Chemistry. 262 (20): 9615–20. doi:10.1016/S0021-9258(18)47978-1. PMID 2885328.

[11] Chesneau V, Pierotti AR, Barré N, Créminon C, Tougard C, Cohen P (January 1994). "Isolation and characterization of a dibasic selective metalloendopeptidase from rat testes that cleaves at the amino terminus of arginine residues". The Journal of Biological Chemistry. 269 (3): 2056–61. doi:10.1016/S0021-9258(17)42134-X. PMID 8294457.

[12] Pierotti AR, Prat A, Chesneau V, Gaudoux F, Leseney AM, Foulon T, Cohen P (June 1994). "N-arginine dibasic convertase, a metalloendopeptidase as a prototype of a class of processing enzymes". Proceedings of the National Academy of Sciences of the United States of America. 91 (13): 6078–82. Bibcode:1994PNAS...91.6078P. doi:10.1073/pnas.91.13.6078. PMC 44141. PMID 8016118.

v t e Proteases: metalloendopeptidases (EC 3.4.24)
ADAM proteins	Alpha secretases ADAM9 ADAM10 ADAM17 ADAM19 ADAM2 ADAM7 ADAM8 ADAM11 ADAM12 ADAM15 ADAM18 ADAM22 ADAM23 ADAM28 ADAM33 ADAMTS1 ADAMTS2 ADAMTS3 ADAMTS4 ADAMTS5 ADAMTS8 ADAMTS9 ADAMTS10 ADAMTS12 ADAMTS13
Matrix metalloproteinases	Collagenases MMP1 MMP8 Gelatinases MMP2 MMP9 MMP3 MMP7 MMP10 MMP11 MMP12 MMP13 MMP14 MMP15 MMP16 MMP17 MMP19 MMP20 MMP21 MMP23A MMP23B MMP24 MMP25 MMP26 MMP27 MMP28
Other	Neprilysin Procollagen peptidase Thermolysin Pappalysin-1 Bone morphogenetic protein 1 Lysostaphin Insulin-degrading enzyme ZMPSTE24

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Nardilysin

Interactions

Enzyme activity

References

Further reading