scholarly journals Circular Permutation of the Native Enzyme-Mediated Cyclization Position in Cyclotides

2020 ◽  
Vol 15 (4) ◽  
pp. 962-969 ◽  
Author(s):  
Bronwyn J. Smithies ◽  
Yen-Hua Huang ◽  
Mark A. Jackson ◽  
Kuok Yap ◽  
Edward K. Gilding ◽  
...  
Keyword(s):  
Circular Permutation ◽  
Native Enzyme

Concanavalin A and Circular Permutation

2010 ◽  
Author(s):  
D.S. Goodsell
Keyword(s):  
Concanavalin A ◽  
Circular Permutation

scholarly journals CPDB: a database of circular permutation in proteins

2008 ◽  
Vol 37 (suppl_1) ◽  
pp. D328-D332 ◽  
Author(s):  
Wei-Cheng Lo ◽  
Chi-Ching Lee ◽  
Che-Yu Lee ◽  
Ping-Chiang Lyu
Keyword(s):  
Circular Permutation

Circular permutation graphs

Networks ◽  
1982 ◽  
Vol 12 (4) ◽  
pp. 429-437 ◽  
Author(s):  
D. Rotem ◽  
J. Urrutia
Keyword(s):  
Circular Permutation ◽  
Permutation Graphs

scholarly journals Engineering the metal-binding loop at a type 1 copper center by circular permutation

RSC Advances ◽  
2017 ◽  
Vol 7 (88) ◽  
pp. 56093-56098
Author(s):  
Honghui Chen ◽  
Binbin Su ◽  
Tongtong Zhang ◽  
Aiping Huang ◽  
Haiping Liu ◽  
...  
Keyword(s):  
Metal Binding ◽  
Circular Permutation ◽  
Type 1 Copper ◽  
Copper Center ◽  
Binding Loop

Circular permutation of the cupredoxin azurin creates a break on the metal binding loop, highlighting the loop's flexibility.

scholarly journals The Structure of a Thermophilic Kinase Shapes Fitness upon Random Circular Permutation

2016 ◽  
Vol 5 (5) ◽  
pp. 415-425 ◽  
Author(s):  
Alicia M. Jones ◽  
Manan M. Mehta ◽  
Emily E. Thomas ◽  
Joshua T. Atkinson ◽  
Thomas H. Segall-Shapiro ◽  
...  
Keyword(s):  
Circular Permutation

scholarly journals The catalase-peroxidase of Synechococcus PCC 7942: purification, nucleotide sequence analysis and expression in Escherichia coli

1996 ◽  
Vol 316 (1) ◽  
pp. 251-257 ◽  
Author(s):  
Michinori MUTSUDA ◽  
Takahiro ISHIKAWA ◽  
Toru TAKEDA ◽  
Shigeru SHIGEOKA
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Molecular Mass ◽  
Peroxidase Activity ◽  
Catalase Activity ◽  
Native Enzyme ◽  
Nucleotide Sequence Analysis ◽  
Synechococcus Pcc 7942 ◽  
Catalase Peroxidase ◽  
Pcc 7942

Synechococcus PCC 7942, a cyanobacterium, possesses catalase–peroxidase as the sole hydrogen peroxide-scavenging system. The enzyme has been purified to electrophoretic homogenenity from the cells. The native enzyme had a molecular mass of 150 kDa and was composed of two identical subunits of molecular mass 79 kDa. The apparent Km value of the catalase activity for H2O2 was 4.2±0.27 mM and the kcat value was 2.6×104 s-1. The enzyme contained high catalase activity and an appreciable peroxidase activity with o-dianisidine and pyrogallol. The catalase activity was not inhibited by 3-amino-1,2,4-triazole but by KCN and NaN3 (apparent Ki values 19.3±0.84 and 20.2±0.95 μM respectively). The enzyme showed an absorption spectrum of typical protohaem and contained one protohaem molecule per dimer. The gene encoding catalase–peroxidase was cloned from the chromosomal DNA of Synechococcus PCC 7942. A 2160 bp open reading frame (ORF), coding a catalase–peroxidase of 720 amino acid residues (approx. 79.9 kDa), was observed. The deduced amino acid sequence coincided with that of the N-terminus of the purified enzyme and showed a remarkable similarity to those of a family of catalase–peroxidases of prokaryotic cells. Escherichia coli BL21(DE3)plysS, harbouring a recombinant plasmid containing the catalase–peroxidase gene, produced a large amount of proteins that co-migrated on SDS/PAGE with the native enzyme. The recombinant enzyme showed the same ratio of catalase activity to peroxidase activity with o-dianisidine and the same Km for H2O2 as the native enzyme.

The interaction of ligands with chemically modified phosphorylase b

1976 ◽  
Vol 54 (5) ◽  
pp. 494-499
Author(s):  
D. Brooks ◽  
S. J. W. Busby ◽  
J. R. Griffiths ◽  
G. K. Radda ◽  
O. Avramovic-Zikic
Keyword(s):  
Conformational Changes ◽  
Spin Label ◽  
Native Enzyme ◽  
Carboxyl Groups ◽  
Chemically Modified ◽  
Allosteric Effector ◽  
Spin Resonance ◽  
Label Probe ◽  
Glycine Ethyl Ester ◽  
Modified Enzyme

Phosphorylase b which had been inactivated with 5-diazo-1H-tetrazole was specifically labelled with 4-iodoacetamidosalicylic acid (a fluorescent probe) or with N-(1-oxyl-2,2,6,6,-tetramethyl-4-piperidinyl)iodoacetamide (a spin label probe) so that the binding of ligands and accompanying conformational changes could be determined by fluorescence or electron spin resonance changes, respectively. The allosteric effector, AMP, causes conformational changes similar to those caused in the native enzyme. The affinity of binding of phosphate or AMP to the inhibited protein is the same as for the unmodified protein. The heterotropic interactions between glucose-1-phosphate or glycogen and AMP are much less in the inactivated enzyme than in unmodified phosphorylase. Using a light scattering assay, it is shown that the modified enzyme binds to glycogen less strongly than the native protein.Phosphorylase b which had been inactivated by carbodiimide in the presence of glycine ethyl ester, resulting in the modification of one or more carboxyl groups, was labelled with the spin label probe described above. The modified enzyme has an affinity for AMP similar to that of the native enzyme. AMP binding to the modified enzyme is tightened by glycogen, weakened by glucose-6-phosphate and is unaffected by glucose- 1-phosphate.The actions of 5-diazo-1H-tetrazole and carbodiimide on phosphorylase are discussed in the light of the above observations.

scholarly journals An Optimal Parallel Algorithm for Constructing a Spanning Tree on Circular Permutation Graphs

2009 ◽  
Vol E92-D (2) ◽  
pp. 141-148 ◽  
Author(s):  
Hirotoshi HONMA ◽  
Saki HONMA ◽  
Shigeru MASUYAMA
Keyword(s):  
Parallel Algorithm ◽  
Spanning Tree ◽  
Circular Permutation ◽  
Permutation Graphs
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