scholarly journals The amino acid sequence of D-ribose-binding protein from Escherichia coli K12.

1983 ◽  
Vol 258 (21) ◽  
pp. 12952-12956 ◽  
Author(s):  
J M Groarke ◽  
W C Mahoney ◽  
J N Hope ◽  
C E Furlong ◽  
F T Robb ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Binding Protein ◽  
Escherichia Coli K12 ◽  
Ribose Binding Protein

scholarly journals The cloning and expression of the aroL gene from Escherichia coli K12. Purification and complete amino acid sequence of shikimate kinase II, the aroL-gene product

1986 ◽  
Vol 237 (2) ◽  
pp. 427-437 ◽  
Author(s):  
G Millar ◽  
A Lewendon ◽  
M G Hunter ◽  
J R Coggins
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Transcriptional Start Site ◽  
Cloning And Expression ◽  
Potential Operator ◽  
Gene Encoding ◽  
Shikimate Kinase ◽  
Complete Amino Acid Sequence ◽  
Escherichia Coli K12

The aroL gene encoding the enzyme shikimate kinase II was cloned from Escherichia coli K12. Construction of over-expressing strains permitted for the first time the purification to homogeneity of a monofunctional shikimate kinase. The complete amino acid sequence of shikimate kinase II was determined by a combined nucleotide and direct amino acid sequencing strategy. E. coli shikimate kinase II is a monomeric enzyme containing 173 amino acid residues with a calculated Mr 18,937. The amino acid sequence contains a region homologous with other kinases and ATP-requiring enzymes. Evidence is presented suggesting that the transcriptional start site of the aroL gene is located within a potential operator site.

Amino acid sequence of the bacterioferritin (gytochrome b1) of Escherichia coli-K12

1989 ◽  
Vol 158 (2) ◽  
pp. 489-496 ◽  
Author(s):  
Simon C. Andrews ◽  
John M.A. Smith ◽  
John R. Guest ◽  
Pauline M. Harrison
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Escherichia Coli K12
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