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CSO S-hydroxycysteine
Glycosylation
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Code : 1FNJ   PDBj   RCSB PDB   PDBe
Header : ISOMERASE
Title : CRYSTAL STRUCTURE ANALYSIS OF CHORISMATE MUTASE MUTANT C88S/R90K
Release Data : 2000-10-11
Compound :
mol_id molecule chains
1 PROTEIN (CHORISMATE MUTASE) A
ec: 5.4.99.5
mutation: YES
Source :
mol_id organism_scientific expression_system
1 Bacillus subtilis  (taxid:1423) Escherichia coli  (taxid:562)
expression_system_vector_type: PLASMID
expression_system_plasmid: PET-22B(+),PKET3-W
Authors : Kast, P., Grisostomi, C., Chen, I.A., Li, S., Krengel, U., Xue, Y., Hilvert, D.
Keywords : chorismate mutase, protein, mutant, pseudo-alpha beta-barrel, trimer, ISOMERASE
Exp. method : X-RAY DIFFRACTION ( 1.90 Å )
Citation :

A strategically positioned cation is crucial for efficient catalysis by chorismate mutase.

Kast, P.,Grisostomi, C.,Chen, I.A.  et al.
(2000)  J.Biol.Chem.  275 : 36832 - 36838

PubMed: 10960481
DOI: 10.1074/jbc.M006351200

Exploring the active site of chorismate mutase by combinatorial mutagenesis and selection: the importance of electrostatic catalysis

Kast, P.,Asif-Ullah, M.,Jiang, N.  et al.
(1996)  Proc.Natl.Acad.Sci.USA  93 : 5043 - 5048

DOI: 10.1073/pnas.93.10.5043

Heavy atom isotope effects reveal a highly polarized transition state for chorismate mutase

Gustin, D.J.,Mattei, P.,Kast, P.  et al.
(1999)  J.Am.Chem.Soc.  121 : 1756 - 1757

DOI: 10.1021/ja9841759

Chain : A
UniProt : P19080 (AROH_BACSU)
Reaction: EC: Evidence:
Physiological Direction:
chorismate = prephenate 5.4.99.5 PubMed:2105742
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