This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3isz
From Proteopedia
m (Protected "3isz" [edit=sysop:move=sysop]) |
Revision as of 09:31, 27 March 2013
Contents |
Crystal structure of mono-zinc form of succinyl-diaminopimelate desuccinylase from Haemophilus influenzae
Template:ABSTRACT PUBMED 20138056
Function
[DAPE_HAEIN] Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls. It can only hydrolyze L,L-N-succinyl-diaminopimelic acid (L,L-SDAP) and is inactive toward D,L-, L,D-, and D,D-SDAP.[1][2][3]
About this Structure
3isz is a 2 chain structure with sequence from Haemophilus influenzae. Full crystallographic information is available from OCA.
Reference
- Nocek BP, Gillner DM, Fan Y, Holz RC, Joachimiak A. Structural basis for catalysis by the mono- and dimetalated forms of the dapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase. J Mol Biol. 2010 Apr 2;397(3):617-26. Epub 2010 Feb 4. PMID:20138056 doi:10.1016/j.jmb.2010.01.062
- ↑ Bienvenue DL, Gilner DM, Davis RS, Bennett B, Holz RC. Substrate specificity, metal binding properties, and spectroscopic characterization of the DapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase from Haemophilus influenzae. Biochemistry. 2003 Sep 16;42(36):10756-63. PMID:12962500 doi:http://dx.doi.org/10.1021/bi034845+
- ↑ Davis R, Bienvenue D, Swierczek SI, Gilner DM, Rajagopal L, Bennett B, Holz RC. Kinetic and spectroscopic characterization of the E134A- and E134D-altered dapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase from Haemophilus influenzae. J Biol Inorg Chem. 2006 Mar;11(2):206-16. Epub 2006 Jan 19. PMID:16421726 doi:10.1007/s00775-005-0071-8
- ↑ Gillner DM, Bienvenue DL, Nocek BP, Joachimiak A, Zachary V, Bennett B, Holz RC. The dapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase from Haemophilus influenzae contains two active-site histidine residues. J Biol Inorg Chem. 2009 Jan;14(1):1-10. doi: 10.1007/s00775-008-0418-z. Epub 2008, Aug 19. PMID:18712420 doi:10.1007/s00775-008-0418-z
Categories: Haemophilus influenzae | Succinyl-diaminopimelate desuccinylase | Gillner, D M. | Holz, R C. | Joachimiak, A. | MCSG, Midwest Center for Structural Genomics. | Nocek, B P. | Amino-acid biosynthesis | Cobalt | Dape | Diaminopimelate biosynthesis | Hydrolase | Lysine biosynthesis | Mcsg | Metal-binding | Metallopeptidase | Midwest center for structural genomic | Protein structure initiative | Psi-2 | Structural genomic | Zn-binding
