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Sequence of NIT1_MOUSE

EC Number:3.5.1.128

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
deaminated glutathione amidase
Q8VDK1
Mus musculus
323
35705
Reaction
N-(4-oxoglutaryl)-L-cysteinylglycine + H2O = 2-oxoglutarate + L-cysteinylglycine
Other sequences found for EC No. 3.5.1.128

General information:

Sequence
show sequence in fasta format
  0 MLGFITRPPH QLLCTGYRLL RTPVLCTQPR PRTMSSSTSW ELPLVAVCQV TSTPNKQENF
 60 KTCAELVQEA ARLGACLAFL PEAFDFIARN PAETLLLSEP LNGDLLGQYS QLARECGIWL
120 SLGGFHERGQ DWEQNQKIYN CHVLLNSKGS VVASYRKTHL CDVEIPGQGP MRESNYTKPG
180 GTLEPPVKTP AGKVGLAICY DMRFPELSLK LAQAGAEILT YPSAFGSVTG PAHWEVLLRA
240 RAIESQCYVI AAAQCGRHHE TRASYGHSMV VDPWGTVVAR CSEGPGLCLA RIDLHFLQQM
300 RQHLPVFQHR RPDLYGSLGH PLS
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
831912
Pekarsky Y.,Campiglio M.,Siprashvili Z.,Druck T.,Sedkov Y.,Tillib S.,Draganescu A.,Wermuth P.,Rothman J.H.,Huebner K.,Buchberg A.M.,Mazo A.,Brenner C.,Croce C.M.
Nitrilase and Fhit homologs are encoded as fusion proteins in Drosophila melanogaster and Caenorhabditis elegans.
Proc. Natl. Acad. Sci. U.S.A.
95
8744-8749
1998
831913
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
831914
Semba S.,Han S.-Y.,Qin H.R.,McCorkell K.A.,Iliopoulos D.,Pekarsky Y.,Druck T.,Trapasso F.,Croce C.M.,Huebner K.
Biological functions of mammalian Nit1, the counterpart of the invertebrate NitFhit Rosetta stone protein, a possible tumor suppressor.
J. Biol. Chem.
281
28244-28253
2006
831915
Jaisson S.,Veiga-da-Cunha M.,Van Schaftingen E.
Molecular identification of omega-amidase, the enzyme that is functionally coupled with glutamine transaminases, as the putative tumor suppressor Nit2.
Biochimie
91
1066-1071
2009
831916
Krasnikov B.F.,Chien C.-H.,Nostramo R.,Pinto J.T.,Nieves E.,Callaway M.,Sun J.,Huebner K.,Cooper A.J.L.
Identification of the putative tumor suppressor Nit2 as omega-amidase, an enzyme metabolically linked to glutamine and asparagine transamination.
Biochimie
91
1072-1080
2009
831917
Zhang H.,Hou Y.-J.,Han S.-Y.,Zhang E.C.,Huebner K.,Zhang J.
Mammalian nitrilase 1 homologue Nit1 is a negative regulator in T cells.
Int. Immunol.
21
691-703
2009
831918
Sun J.,Okumura H.,Yearsley M.,Frankel W.,Fong L.Y.,Druck T.,Huebner K.
Nit1 and Fhit tumor suppressor activities are additive.
J. Cell. Biochem.
107
1097-1106
2009
831919
Huttlin E.L.,Jedrychowski M.P.,Elias J.E.,Goswami T.,Rad R.,Beausoleil S.A.,Villen J.,Haas W.,Sowa M.E.,Gygi S.P.
A tissue-specific atlas of mouse protein phosphorylation and expression.
Cell
143
1174-1189
2010
831920
Peracchi A.,Veiga-da-Cunha M.,Kuhara T.,Ellens K.W.,Paczia N.,Stroobant V.,Seliga A.K.,Marlaire S.,Jaisson S.,Bommer G.T.,Sun J.,Huebner K.,Linster C.L.,Cooper A.J.L.,Van Schaftingen E.
Nit1 is a metabolite repair enzyme that hydrolyzes deaminated glutathione.
Proc. Natl. Acad. Sci. U.S.A.
114
0-0
2017