Comparison of human glutamate carboxypeptidases II and III reveals their divergent substrate specificities

Author:

Navrátil Michal12,Tykvart Jan12,Schimer Jiří12,Pachl Petr1,Navrátil Václav12,Rokob Tibor András3,Hlouchová Klára12,Rulíšek Lubomír1,Konvalinka Jan12

Affiliation:

1. Institute of Organic Chemistry and Biochemistry; Gilead Sciences and IOCB Research Centre; Academy of Sciences of the Czech Republic; Prague Czech Republic

2. Department of Biochemistry; Faculty of Natural Sciences; Charles University in Prague; Czech Republic

3. Institute of Organic Chemistry; Research Centre for Natural Sciences; Hungarian Academy of Sciences; Budapest Hungary

Funder

Grantová Agentura České Republiky

InterBioMed I

Ministry of Education of the Czech Republic

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference53 articles.

1. GCPII variants, paralogs and orthologs;Hlouchova;Curr Med Chem,2012

2. Isolation and expression of novel human glutamate carboxypeptidases with N-acetylated alpha-linked acidic dipeptidase and dipeptidyl peptidase IV activity;Pangalos;J Biol Chem,1999

3. Biochemical characterization of human glutamate carboxypeptidase III;Hlouchova;J Neurochem,2007

4. The cloning and characterization of a second brain enzyme with NAAG peptidase activity;Bzdega;J Neurochem,2004

5. Hydrolysis of the brain dipeptide N-acetyl-L-aspartyl-L-glutamate. Identification and characterization of a novel N-acetylated alpha-linked acidic dipeptidase activity from rat brain;Robinson;J Biol Chem,1987

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