Sequence of CBPA2_RAT
EC Number:3.4.17.15
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
Similar to that of carboxypeptidase A (EC 3.4.17.1), but with a preference for bulkier C-terminal residues
Other sequences found for EC No. 3.4.17.15
General information:
Sequence
0 MRLTLLLAAL LGYIYCQETF VGDQVLEIIP SHEEQIRTLL QLEAEEHLEL DFWKSPTIPG
60 ETVHVRVPFA SIQAVKVFLE SQGIDYSIMI EDVQVLLDQE REEMLFNQQR ERGGNFNFEA
120 YHTLEEIYQE MDNLVAENPG LVSKVNLGSS FENRPMNVLK FSTGGDKPAI WLDAGIHARE
180 WVTQATALWT ANKIASDYGT DPAITSLLNT LDIFLLPVTN PDGYVFSQTT NRMWRKTRSK
240 RSGSGCVGVD PNRNWDANFG GPGASSSPCS DSYHGPKPNS EVEVKSIVDF IKSHGKVKAF
300 ITLHSYSQLL MFPYGYKCTK PDDFNELDEV AQKAAQALKR LHGTSYKVGP ICSVIYQASG
360 GSIDWAYDLG IKYSFAFELR DTAFYGFLLP AKQILPTAEE TWLGLKTIME HVRDHPY
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
907370
Gardell S.J.,Craik C.S.,Clauser E.,Goldsmith E.J.,Stewart C.-B.,Graf M.,Rutter W.J.
A novel rat carboxypeptidase, CPA2: characterization, molecular cloning, and evolutionary implications on substrate specificity in the carboxypeptidase gene family.
J. Biol. Chem.
263
17828-17836
1988
907371
Normant E.,Gros C.,Schwartz J.C.
Carboxypeptidase A isoforms produced by distinct genes or alternative splicing in brain and other extrapancreatic tissues.
J. Biol. Chem.
270
20543-20549
1995
907372
Faming Z.,Kobe B.,Stewart C.-B.,Rutter W.J.,Goldsmith E.J.
Structural evolution of an enzyme specificity. The structure of rat carboxypeptidase A2 at 1.9-A resolution.
J. Biol. Chem.
266
24606-24612
1991
