scholarly journals Biochemical characterization of the class B acid phosphatase (AphA) of Escherichia coli MG1655

2006 ◽  
Vol 1764 (1) ◽  
pp. 13-19 ◽  
Author(s):  
Claudio Passariello ◽  
Costantino Forleo ◽  
Vanna Micheli ◽  
Serena Schippa ◽  
Rosalida Leone ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Acid Phosphatase ◽  
Biochemical Characterization ◽  
Class B

scholarly journals Identification of the gene (aphA) encoding the class B acid phosphatase/phosphotransferase of Escherichia coli MG1655 and characterization of its product

2006 ◽  
Vol 146 (2) ◽  
pp. 191-198 ◽  
Author(s):  
Maria Cristina Thaller ◽  
Serena Schippa ◽  
Alessandra Bonci ◽  
Stefania Cresti ◽  
Gian Maria Rossolini
Keyword(s):  
Escherichia Coli ◽  
Acid Phosphatase ◽  
Class B

Purification and biochemical characterization of a recombinant Anopheles gambiae tryptophan 2,3-dioxygenase expressed in Escherichia coli

2008 ◽  
Vol 38 (9) ◽  
pp. 871-876 ◽  
Author(s):  
Alessandra Paglino ◽  
Fabrizio Lombardo ◽  
Bruno Arcà ◽  
Menico Rizzi ◽  
Franca Rossi
Keyword(s):  
Escherichia Coli ◽  
Anopheles Gambiae ◽  
Biochemical Characterization

Biochemical characterization of the tartrate-resistant acid phosphatase of human spleen with leukemic reticuloendotheliosis as a pyrophosphatase.

1977 ◽  
Vol 23 (1) ◽  
pp. 89-94 ◽  
Author(s):  
K W Lam ◽  
L T Yam
Keyword(s):  
Acid Phosphatase ◽  
Biochemical Characterization ◽  
Normal Animal ◽  
Tartrate Resistant Acid Phosphatase ◽  
Animal Tissues ◽  
Human Spleen ◽  
Optimal Activity ◽  
Catalytic Function ◽  
Hydrolysis Of

Abstract A tartrate-resistant acid phosphatase was isolated from a human leukemic spleen by freeze-thawing in saline and purified by repeated chromatography on carboxymethyl-cellulose. The purified enzyme has a molecular weight of 64 000. It catalyzes the hydrolysis of inorganic and organic pyrophosphate as well as the phenolic ester of monoorthophosphate, with optimal activity between pH 5 and 6. However, there is no activity toward mono-orthophosphate esters of aliphatic alcohols. The present data have identified its catalytic function as a pyrophosphatase. However, it has properties different from the pyrophosphatase previously observed in normal animal tissues.

scholarly journals Molecular and Biochemical Characterization of the xlnD-Encoded 3-Hydroxybenzoate 6-Hydroxylase Involved in the Degradation of 2,5-Xylenol via the Gentisate Pathway in Pseudomonas alcaligenes NCIMB 9867

2005 ◽  
Vol 187 (22) ◽  
pp. 7696-7702 ◽  
Author(s):  
Xiaoli Gao ◽  
Chew Ling Tan ◽  
Chew Chieng Yeo ◽  
Chit Laa Poh
Keyword(s):  
Escherichia Coli ◽  
Fusion Protein ◽  
Molecular Mass ◽  
Electron Donor ◽  
Biochemical Characterization ◽  
Aromatic Substrates ◽  
Gentisate Pathway ◽  
A Subunit ◽  
Pseudomonas Alcaligenes

ABSTRACT The xlnD gene from Pseudomonas alcaligenes NCIMB 9867 (strain P25X) was shown to encode 3-hydroxybenzoate 6-hydroxylase I, the enzyme that catalyzes the NADH-dependent conversion of 3-hydroxybenzoate to gentisate. Active recombinant XlnD was purified as a hexahistidine fusion protein from Escherichia coli, had an estimated molecular mass of 130 kDa, and is probably a trimeric protein with a subunit mass of 43 kDa. This is in contrast to the monomeric nature of the few 3-hydroxybenzoate 6-hydroxylases that have been characterized thus far. Like other 3-hydroxybenzoate 6-hydroxylases, XlnD could utilize either NADH or NADPH as the electron donor. P25X harbors a second 3-hydroxybenzoate 6-hydroxylase II that was strictly inducible by specific aromatic substrates. However, the degradation of 2,5-xylenol and 3,5-xylenol in strain P25X was found to be dependent on the xlnD-encoded 6-hydroxylase I and not the second, strictly inducible 6-hydroxylase II.

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