A Histidine Residue in the Catalytic Mechanism DistinguishesVibrioharveyiAldehyde Dehydrogenase from Other Members of the Aldehyde Dehydrogenase Superfamily†

Biochemistry ◽  
2000 ◽  
Vol 39 (47) ◽  
pp. 14409-14418 ◽  
Author(s):  
Lei Zhang ◽  
Bijan Ahvazi ◽  
Rose Szittner ◽  
Alice Vrielink ◽  
Edward Meighen
Keyword(s):  
Aldehyde Dehydrogenase ◽  
Catalytic Mechanism ◽  
Histidine Residue ◽  
Aldehyde Dehydrogenase Superfamily

scholarly journals Structures of Proline Utilization A (PutA) Reveal the Fold and Functions of the Aldehyde Dehydrogenase Superfamily Domain of Unknown Function

2016 ◽  
Vol 291 (46) ◽  
pp. 24065-24075 ◽  
Author(s):  
Min Luo ◽  
Thameesha T. Gamage ◽  
Benjamin W. Arentson ◽  
Katherine N. Schlasner ◽  
Donald F. Becker ◽  
...  
Keyword(s):  
Aldehyde Dehydrogenase ◽  
Unknown Function ◽  
Aldehyde Dehydrogenase Superfamily ◽  
Proline Utilization ◽  
Domain Of Unknown Function ◽  
Proline Utilization A

Triosephosphate isomerase: removal of a putatively electrophilic histidine residue results in a subtle change in catalytic mechanism

Biochemistry ◽  
1988 ◽  
Vol 27 (16) ◽  
pp. 5948-5960 ◽  
Author(s):  
Elliott B. Nickbarg ◽  
Robert C. Davenport ◽  
Gregory A. Petsko ◽  
Jeremy R. Knowles
Keyword(s):  
Triosephosphate Isomerase ◽  
Catalytic Mechanism ◽  
Histidine Residue ◽  
Subtle Change

Testimony of the Correlation Between the Reactive Histidine Residue and the Arginase Catalytic Mechanism Using a Biochromatographic Concept and Mutagenesis Experiments

2008 ◽  
Vol 68 (9-10) ◽  
pp. 807-810
Author(s):  
Claire André ◽  
Teddy Bagnost ◽  
Samuel Limat ◽  
Tijani Gharbi ◽  
Yves Claude Guillaume
Keyword(s):  
Catalytic Mechanism ◽  
Histidine Residue

scholarly journals Catalytic mechanism of the phospholipase D superfamily proceeds via a covalent phosphohistidine intermediate

1998 ◽  
Vol 95 (16) ◽  
pp. 9202-9207 ◽  
Author(s):  
Elizabeth B. Gottlin ◽  
Amy E. Rudolph ◽  
Yi Zhao ◽  
Harry R. Matthews ◽  
Jack E. Dixon
Keyword(s):  
Amino Acid ◽  
Phospholipase D ◽  
Inorganic Phosphate ◽  
Pathogenic Bacteria ◽  
Water Exchange ◽  
Catalytic Mechanism ◽  
Phospholipid Metabolism ◽  
Nucleophilic Attack ◽  
Sequence Motif ◽  
Histidine Residue

The phospholipase D (PLD) superfamily includes enzymes of phospholipid metabolism, nucleases, as well as ORFs of unknown function in viruses and pathogenic bacteria. These enzymes are characterized by the invariant sequence motif, H(X)K(X)4D. The endonuclease member Nuc of the PLD family was over-expressed in bacteria and purified to homogeneity. Mutation of the conserved histidine to an asparagine in the endonuclease reduced the kcat for hydrolysis by a factor of 105, suggesting that the histidine residue plays a key role in catalysis. In addition to catalyzing hydrolysis, a number of phosphohydrolases will catalyze a phosphate (oxygen)-water exchange reaction. We have taken advantage of this observation and demonstrate that a 32P-labeled protein could be trapped when the enzyme was incubated with 32P-labeled inorganic phosphate. The phosphoenzyme intermediate was stable in 1 M NaOH and labile in 1 M HCl and 1 M hydroxylamine, suggesting that the enzyme forms a phosphohistidine intermediate. The pH-stability profile of the phosphoenzyme intermediate was consistent with phosphohistidine and the only radioactive amino acid found after alkaline hydrolysis was phosphohistidine. These results suggest that the enzymes in the PLD superfamily use the conserved histidine for nucleophilic attack on the substrate phosphorus atom and most likely proceed via a common two-step catalytic mechanism.

Aldehyde Dehydrogenase Catalytic Mechanism

1999 ◽  
pp. 53-59 ◽  
Author(s):  
John Hempel ◽  
John Perozich ◽  
Toby Chapman ◽  
John Rose ◽  
Josette S. Boesch ◽  
...  
Keyword(s):  
Aldehyde Dehydrogenase ◽  
Catalytic Mechanism
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