scholarly journals Purification and properties of cytochrome b556 in the respiratory chain of aerobically grown Escherichia coli K12.

1978 ◽  
Vol 253 (24) ◽  
pp. 8910-8915
Author(s):  
K. Kita ◽  
I. Yamato ◽  
Y. Anraku
Keyword(s):  
Escherichia Coli ◽  
Respiratory Chain ◽  
Escherichia Coli K12 ◽  
Purification And Properties

scholarly journals Purification and properties of d-ribulokinase and d-xylulokinase from Klebsiella aerogenes

1981 ◽  
Vol 193 (2) ◽  
pp. 513-524 ◽  
Author(s):  
M S Neuberger ◽  
B S Hartley ◽  
J E Walker
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Klebsiella Aerogenes ◽  
Amino Acid Compositions ◽  
Escherichia Coli K12 ◽  
Purification And Properties

The D-ribulokinase and D-xylulokinase of Klebsiella aerogenes were purified to homogeneity from Escherichia coli K12 construct strains that synthesized these enzymes constitutively. The D-ribulokinase, which is encoded in the ribitol operon, is active as a dimer of 60 000 subunit mol.wt., whereas the D-xylulokinase, which is encoded in the D-arabitol operon, is active as a dimer of 54 000 subunit mol.wt. The amino acid compositions and N-terminal sequences of both pentulokinases are reported. The Kapp. values of the enzymes for their D-pentulose substrates were determined, and the D-ribulokinase was shown to have a low-affinity side-specificity for ribitol and D-arabitol. These results are discussed in the context of the evolution of the Klebsiella aerogenes pentitol operons.

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