Genomes and Genes
Citrobacter koseri ATCC BAA-895
Alias: Citrobacter (diversus) koseri ATCC BAA-895, Citrobacter koseri str. ATCC BAA-895, Citrobacter koseri strain ATCC BAA-895
- 3'-Phosphoadenosine-5'-phosphosulfate reductase in complex with thioredoxin: a structural snapshot in the catalytic cycleJustin Chartron
Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA
Biochemistry 46:3942-51. 2007....
- Structures of apo- and holo-tyrosine phenol-lyase reveal a catalytically critical closed conformation and suggest a mechanism for activation by K+ ionsDalibor Milić
Department of Chemistry, Faculty of Science, University of Zagreb, Horvatovac 102a, HR 10000 Zagreb, Croatia
Biochemistry 45:7544-52. 2006..Finally, the closed conformation allows us to model keto(imino)quinonoid, the key transition intermediate...
- Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate bindingM Eriksson
Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala Biomedical Center, Sweden
Structure 5:1077-92. 1997..Our aim has been to crystallographically demonstrate substrate binding and to locate the two effector-binding sites...
- Structure of Citrobacter freundii L-methionine gamma-lyaseD V Mamaeva
Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov str 32, 119991 Moscow, Russia
Acta Crystallogr Sect F Struct Biol Cryst Commun 61:546-9. 2005..The comparison of these structures revealed that there are differences in PLP-binding residues and positioning of the surrounding flexible loops...
- A new mechanism-based radical intermediate in a mutant R1 protein affecting the catalytically essential Glu441 in Escherichia coli ribonucleotide reductaseA L Persson
Department of Molecular Biology, Stockholm University, Stockholm, Sweden
J Biol Chem 272:31533-41. 1997....
- Three-dimensional structure of tyrosine phenol-lyaseA A Antson
Shubnikov Institute of Crystallography, Russian Academy of Sciences, Moscow
Biochemistry 32:4195-206. 1993....
- QnrB9 in association with TEM-116 extended-spectrum beta-lactamase in Citrobacter freundii isolated from sewage effluent: first report from ItalyC Forcella
Dipartimento di Scienze e Tecnologie Biomediche, University of L Aquila, Italy
J Chemother 22:243-5. 2010..This is the first finding in Italy of qnrB9 and TEM-116 in a non-clinical or animal strain...
- NMR structure of Citrobacter freundii AmpD, comparison with bacteriophage T7 lysozyme and homology with PGRP domainsEdvards Liepinsh
Department of Medical Biochemistry, Karolinska Institute, S 17177 Stockholm, Sweden
J Mol Biol 327:833-42. 2003..This hypothesis is supported by the observation that human serum N-acetylmuramyl-L-alanine amidase seems to be identical with a soluble form of human PGRP-L...
- The catalytic mechanism of tyrosine phenol-lyase from Erwinia herbicola: the effect of substrate structure on pH-dependence of kinetic parameters in the reactions with ring-substituted tyrosinesN G Faleev
Institue of Food Substances, Russian Academy of Sciences, Moscow, Russia
Z Naturforsch C 51:363-70. 1996..The activity of Citrobacter enzyme towards DOPA is considerably less than that of E. herbicola enzyme, and its maximal value is attained at higher pH...
- Insights into enzyme evolution revealed by the structure of methylaspartate ammonia lyaseC W Levy
Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, The University of Sheffield, Sheffield S10 2TN, United Kingdom
Structure 10:105-13. 2002..This analysis resolves the conflict that had linked MAL to the histidine and phenylalanine ammonia lyase family of enzymes...
- The polypeptide chain fold in tyrosine phenol-lyase, a pyridoxal-5'-phosphate-dependent enzymeA A Antson
European Molecular Biology Laboratory, DESY, Hamburg, Germany
FEBS Lett 302:256-60. 1992..Each subunit consists of two domains. The topology of the large domain appears to be similar to that of the aminotransferases...
- The crystal structure of Citrobacter freundii tyrosine phenol-lyase complexed with 3-(4'-hydroxyphenyl)propionic acid, together with site-directed mutagenesis and kinetic analysis, demonstrates that arginine 381 is required for substrate specificityB Sundararaju
Department of Chemistry, Center for Metalloenzyme Studies, University of Georgia, Athens 30602, USA
Biochemistry 36:6502-10. 1997..M., & Phillips. R. S. (1988) Biochemistry 27, 7333-7338], and hence Arg 381 is at least partially responsible for the substrate specificity of TPL...
- Structure of ribonucleotide reductase protein R1U Uhlin
Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala
Nature 370:533-9. 1994..The fifth cysteine, in a loop in the centre of the barrel, is positioned to initiate the radical reaction...