Molecular Cloning of a Novel Human Acid Phosphatase Gene (ACPT) That Is Highly Expressed in the Testis

Genomics ◽  
2001 ◽  
Vol 74 (3) ◽  
pp. 385-395 ◽  
Author(s):  
George M. Yousef ◽  
Maria Diamandis ◽  
Klaus Jung ◽  
Eleftherios P. Diamandis
Keyword(s):  
Acid Phosphatase ◽  
Molecular Cloning ◽  
Human Acid ◽  
Acid Phosphatase Gene

Immunological characterization of human acid phosphatase gene products

1985 ◽  
Vol 23 (3-4) ◽  
pp. 309-319 ◽  
Author(s):  
Abdul Waheed ◽  
Robert L. Van Etten ◽  
V. Gieselmann ◽  
K. von Figura
Keyword(s):  
Acid Phosphatase ◽  
Gene Products ◽  
Immunological Characterization ◽  
Human Acid ◽  
Acid Phosphatase Gene

Confirmation of the Assignment of the Human Tartrate-Resistant Acid Phosphatase Gene (ACP5) to Chromosome 19

Genomics ◽  
1994 ◽  
Vol 19 (1) ◽  
pp. 180-181 ◽  
Author(s):  
Robin J. Leach ◽  
Bonnie E. Reus ◽  
Jeffrey E. Hundley ◽  
Teresa L. Johnson-Pais ◽  
Jolene J. Windle
Keyword(s):  
Acid Phosphatase ◽  
Tartrate Resistant Acid Phosphatase ◽  
Chromosome 19 ◽  
Acid Phosphatase Gene

scholarly journals Phosphorylation of Nucleosides by the Mutated Acid Phosphatase from Morganella morganii

2000 ◽  
Vol 66 (7) ◽  
pp. 2811-2816 ◽  
Author(s):  
Yasuhiro Mihara ◽  
Takashi Utagawa ◽  
Hideaki Yamada ◽  
Yasuhisa Asano
Keyword(s):  
Acid Phosphatase ◽  
Random Mutagenesis ◽  
Reaction Yield ◽  
Mutant Library ◽  
Morganella Morganii ◽  
Gene Encoding ◽  
E Coli ◽  
Acid Phosphatase Gene ◽  
Phosphate Source

ABSTRACT A novel nucleoside phosphorylation process using the food additive pyrophosphate as the phosphate source was investigated. TheMorganella morganii gene encoding a selective nucleoside pyrophosphate phosphotransferase was cloned. It was identical to theM. morganii PhoC acid phosphatase gene. Sequential in vitro random mutagenesis was performed on the gene by error-prone PCR to construct a mutant library. The mutant library was introduced intoEscherichia coli, and the transformants were screened for the production of 5′-IMP. One mutated acid phosphatase with an increased phosphotransferase reaction yield was obtained. With E. coli overproducing the mutated acid phosphatase, 101 g of 5′-IMP per liter (192 mM) was synthesized from inosine in an 88% molar yield. This improvement was achieved with two mutations, Gly to Asp at position 92 and Ile to Thr at position 171. A decreasedKm value for inosine was responsible for the increased productivity.

scholarly journals Signal peptide specificity in posttranslational processing of the plant protein phaseolin in Saccharomyces cerevisiae.

1987 ◽  
Vol 7 (1) ◽  
pp. 121-128 ◽  
Author(s):  
J H Cramer ◽  
K Lea ◽  
M D Schaber ◽  
R A Kramer
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Acid Phosphatase ◽  
Signal Peptide ◽  
Regulatory Region ◽  
Cellular Protein ◽  
Proteolytic Processing ◽  
Coding Region ◽  
Molecular Weights ◽  
Amino Terminal ◽  
Acid Phosphatase Gene

We linked the cDNA coding region for the bean storage protein phaseolin to the promoter and regulatory region of the Saccharomyces cerevisiae repressible acid phosphatase gene (PHO5) in multicopy expression plasmids. Yeast transformants containing these plasmids expressed phaseolin at levels up to 3% of the total soluble cellular protein. Phaseolin polypeptides in S. cerevisiae were glycosylated, and their molecular weights suggested that the signal peptide had been processed. We also constructed a series of plasmids in which the phaseolin signal-peptide-coding region was either removed or replaced with increasing amounts of the amino-terminal coding region for acid phosphatase. Phaseolin polypeptides with no signal peptide were not posttranslationally modified in S. cerevisiae. Partial or complete substitution of the phaseolin signal peptide with that from acid phosphatase dramatically inhibited both signal peptide processing and glycosylation, suggesting that some specific feature of the phaseolin signal amino acid sequence was required for these modifications to occur. Larger hybrid proteins that included approximately one-half of the acid phosphatase sequence linked to the amino terminus of the mature phaseolin polypeptide did undergo proteolytic processing and glycosylation. However, these polypeptides were cleaved at several sites that are not normally used in the unaltered acid phosphatase protein.

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