scholarly journals Cysteine scanning mutagenesis of the N-terminal 32 amino acid residues in the lactose permease of Escherichia coli

1994 ◽  
Vol 3 (2) ◽  
pp. 240-247 ◽  
Author(s):  
Miklós Sahin-Tóth ◽  
Bengt Persson ◽  
Jeremy Schwieger ◽  
Pejman Cohan ◽  
H.Ronald Kaback
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Lactose Permease ◽  
Amino Acid Residues ◽  
Cysteine Scanning ◽  
Cysteine Scanning Mutagenesis

Cysteine-Scanning Mutagenesis of Putative Helix VII in the Lactose Permease of Escherichia coli

Biochemistry ◽  
1994 ◽  
Vol 33 (26) ◽  
pp. 8074-8081 ◽  
Author(s):  
Stathis Frillingos ◽  
Miklos Sahin-Toth ◽  
Bengt Persson ◽  
H. Ronald Kaback
Keyword(s):  
Escherichia Coli ◽  
Lactose Permease ◽  
Cysteine Scanning ◽  
Cysteine Scanning Mutagenesis

Cysteine scanning mutagenesis of putative helix XI in the lactose permease of Escherichia coli

Biochemistry ◽  
1993 ◽  
Vol 32 (47) ◽  
pp. 12644-12650 ◽  
Author(s):  
Rhonda L. Dunten ◽  
Miklos Sahin-Toth ◽  
H. Ronald Kaback
Keyword(s):  
Escherichia Coli ◽  
Lactose Permease ◽  
Cysteine Scanning ◽  
Cysteine Scanning Mutagenesis

Expression and partial purification of human pro-opiomelanocortin in Escherichia coli

1989 ◽  
Vol 3 (2) ◽  
pp. 105-112 ◽  
Author(s):  
T. S. Grewal ◽  
P. J. Lowry ◽  
D. Savva
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Fusion Protein ◽  
Western Blot ◽  
Blot Analysis ◽  
Expression Vectors ◽  
Partial Purification ◽  
Amino Acid Residues ◽  
E Coli ◽  
Dna Fragment

ABSTRACT A large portion of the human pro-opiomelanocortin (POMC) peptide corresponding to amino acid residues 59–241 has been cloned and expressed in Escherichia coli. A 1·0 kb DNA fragment encoding this peptide was cloned into the expression vectors pUC8 and pUR291. Plasmid pJMBG51 (a pUC8 recombinant) was found to direct the expression of a 24 kDa peptide. The recombinant pUR291 (pJMBG52) was shown to produce a β-galactosidase fusion protein of 140 kDa. Western blot analysis showed that both the 24 kDa and 140 kDa peptides are recognized by antibodies raised against POMC-derived peptides. The β-galactosidase fusion protein has been partially purified from crude E. coli cell lysates using affinity chromatography on p-aminobenzyl-1-thio-β-d-galactopyranoside agarose.

Developing structure-based models to predict substrate specificity of D-group (Type II) molybdenum enzymes: application to a molybdo-enzyme of unknown function from Archaeoglobus fulgidus

2006 ◽  
Vol 34 (1) ◽  
pp. 118-121 ◽  
Author(s):  
E.J. Dridge ◽  
D.J. Richardson ◽  
R.J. Lewis ◽  
C.S. Butler
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Sequence Analysis ◽  
Archaeoglobus Fulgidus ◽  
Substrate Selectivity ◽  
Type Ii ◽  
Amino Acid Residues ◽  
Sequence Alignments ◽  
X Ray ◽  
Group Type

The AF0174–AF0176 gene cluster in Archaeoglobus fulgidus encodes a putative oxyanion reductase of the D-type (Type II) family of molybdo-enzymes. Sequence analysis reveals that the catalytic subunit AF0176 shares low identity (31–32%) and similarity (41–42%) to both NarG and SerA, the catalytic components of the respiratory nitrate and selenate reductases respectively. Consequently, predicting the oxyanion substrate selectivity of AF0176 has proved difficult based solely on sequence alignments. In the present study, we have modelled both AF0176 and SerA on the recently determined X-ray structure of the NAR (nitrate reductase) from Escherichia coli and have identified a number of key amino acid residues, conserved in all known NAR sequences, including AF0176, that we speculate may enhance selectivity towards trigonal planar (NO3−) rather than tetrahedral (SeO42− and ClO4−) substrates.

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