Reporter group at the active site of acetoacetate decarboxylase. I. Ionization constant of the nitrophenol

1971 ◽  
Vol 93 (26) ◽  
pp. 7266-7269 ◽  
Author(s):  
Perry A. Frey ◽  
Fritz C. Kokesh ◽  
F. H. Westheimer
Keyword(s):  
Active Site ◽  
Ionization Constant ◽  
Acetoacetate Decarboxylase ◽  
Reporter Group

Reaction of the active site of papain with a reporter group labeled phenacyl halide

1970 ◽  
Vol 92 (23) ◽  
pp. 6980-6982 ◽  
Author(s):  
Emil T. Kaiser ◽  
Richard W. Furlanetto
Keyword(s):  
Active Site ◽  
Reporter Group

pK of the lysine amino group at the active site of acetoacetate decarboxylase

Biochemistry ◽  
1971 ◽  
Vol 10 (7) ◽  
pp. 1249-1253 ◽  
Author(s):  
Frank H. Westheimer ◽  
Donald E. Schmidt
Keyword(s):  
Active Site ◽  
Amino Group ◽  
Acetoacetate Decarboxylase

Environment of a reporter group at the active site of chymotrypsin

1967 ◽  
Vol 89 (23) ◽  
pp. 5945-5951 ◽  
Author(s):  
Merrill B. Hille ◽  
Daniel E. Koshland
Keyword(s):  
Active Site ◽  
Reporter Group

scholarly journals Swit_4259, an acetoacetate decarboxylase-like enzyme from Sphingomonas wittichii RW1

2017 ◽  
Vol 73 (12) ◽  
pp. 672-681 ◽  
Author(s):  
Lisa S. Mydy ◽  
Zahra Mashhadi ◽  
T. William Knight ◽  
Tyler Fenske ◽  
Trevor Hagemann ◽  
...  
Keyword(s):  
Active Site ◽  
Tertiary Structure ◽  
Gene Clusters ◽  
Decarboxylase Activity ◽  
Negative Bacterium ◽  
Genomic Context ◽  
The Family ◽  
Acetoacetate Decarboxylase ◽  
Sphingomonas Wittichii ◽  
Dehydratase Activity

The Gram-negative bacterium Sphingomonas wittichii RW1 is notable for its ability to metabolize a variety of aromatic hydrocarbons. Not surprisingly, the S. wittichii genome contains a number of putative aromatic hydrocarbon-degrading gene clusters. One of these includes an enzyme of unknown function, Swit_4259, which belongs to the acetoacetate decarboxylase-like superfamily (ADCSF). Here, it is reported that Swit_4259 is a small (28.8 kDa) tetrameric ADCSF enzyme that, unlike the prototypical members of the superfamily, does not have acetoacetate decarboxylase activity. Structural characterization shows that the tertiary structure of Swit_4259 is nearly identical to that of the true decarboxylases, but there are important differences in the fine structure of the Swit_4259 active site that lead to a divergence in function. In addition, it is shown that while it is a poor substrate, Swit_4259 can catalyze the hydration of 2-oxo-hex-3-enedioate to yield 2-oxo-4-hydroxyhexanedioate. It is also demonstrated that Swit_4259 has pyruvate aldolase-dehydratase activity, a feature that is common to all of the family V ADCSF enzymes studied to date. The enzymatic activity, together with the genomic context, suggests that Swit_4259 may be a hydratase with a role in the metabolism of an as-yet-unknown hydrocarbon. These data have implications for engineering bioremediation pathways to degrade specific pollutants, as well as structure–function relationships within the ADCSF in general.

scholarly journals Preferential nitration with tetranitromethane of a specific tyrosine residue in penicillinase from Staphylococcus aureus PCl. Evidence that the preferentially nitrated residue is not part of the active site but that loss of activity is due to intermolecular cross-linking

1978 ◽  
Vol 169 (2) ◽  
pp. 381-388 ◽  
Author(s):  
A F Bristow ◽  
R Virden
Keyword(s):  
Catalytic Activity ◽  
Active Site ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Normal Activity ◽  
Enzymic Activity ◽  
Cross Linking ◽  
Partial Loss ◽  
Tyrosine Residues ◽  
Reporter Group

1. Nitration of tyrosine residues of staphylococal penicillinase was accompanied by a partial loss of enzymic activity, which was not readily explained by nitration of a single residue. 2. Loss of activity correlated with low recovery of tyrosine plus nitrotyrosine, which was consistent with cross-linking. 3. The fraction of treated enzyme that was eluted from Sephadex G-75 earlier than native penicillinase was similar to the fraction of enzyme activity lost. Protein eluted in positions corresponding to monomer, dimer and higher oligomers respectively showed major bands in corresponding positions in sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, indicating that the increase in molecular weight was due to intermolecular cross-linking. Monomeric enzyme containing up to 4 mol of nitrotyrosine/mol retained full catalytic activity. Dimeric enzyme retained 50% of normal activity, whereas higher oligomers retained an average of 8-15% of normal activity. 4. Monomeric enzyme isolated after treatment with equimolar tetranitromethane was nitrated predominantly at tyrosine-72.5. Reaction of reduced nitrated monomer with 1,5-difluoro-2,4-dinitrobenzene gave a monomeric, apparently cross-linked product with full catalytic activity. 6. It is concluded that tyrosine-72 plays no part in the active site. Its preferential nitration may be due to its being insufficiently exposed to be available for intermolecular cross-linking. This poperty may make it useful for attachment of a reporter group.

A Novel Restricted Photoaffinity Spin-Labeled Non-Nucleoside ATP Analogue as a Covalently Attached Reporter Group of the Active Site of Myosin Subfragment 1†

Biochemistry ◽  
2002 ◽  
Vol 41 (8) ◽  
pp. 2609-2620 ◽  
Author(s):  
Xiaoru Chen ◽  
Jean Grammer ◽  
J. David Lawson ◽  
Roger Cooke ◽  
Edward Pate ◽  
...  
Keyword(s):  
Active Site ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1 ◽  
Reporter Group
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