Human PHOSPHO1 exhibits high specific phosphoethanolamine and phosphocholine phosphatase activities

Scott J Roberts; Alan J Stewart; Peter J Sadler; Colin Farquharson

doi:10.1042/BJ20040511

Human PHOSPHO1 exhibits high specific phosphoethanolamine and phosphocholine phosphatase activities

Scott J Roberts, Alan J Stewart, Peter J Sadler, Colin Farquharson

Royal (Dick) School of Veterinary Studies

Research output: Contribution to journal › Article › peer-review

Abstract / Description of output

Human PHOSPHO1 is a phosphatase enzyme for which expression is upregulated in mineralizing cells. This enzyme has been implicated in the generation of P(i) for matrix mineralization, a process central to skeletal development. PHOSPHO1 is a member of the haloacid dehalogenase (HAD) superfamily of Mg2+-dependent hydrolases. However, substrates for PHOSPHO1 are, as yet, unidentified and little is known about its activity. We show here that PHOSPHO1 exhibits high specific activities toward phosphoethanolamine (PEA) and phosphocholine (PCho). Optimal enzymic activity was observed at approx. pH 6.7. The enzyme shows a high specific Mg2+-dependence, with apparent K(m) values of 3.0 microM for PEA and 11.4 microM for PCho. These results provide a novel mechanism for the generation of P(i) in mineralizing cells from PEA and PCho.

Original language	English
Pages (from-to)	59-65
Number of pages	7
Journal	Biochemical Journal
Volume	382
Issue number	Pt 1
DOIs	https://doi.org/10.1042/BJ20040511
Publication status	Published - 15 Aug 2004

Keywords / Materials (for Non-textual outputs)

Cell Line, Tumor
Ethanolamines
Humans
Metals
Osteosarcoma
Phosphoric Monoester Hydrolases
Phosphorylcholine
Recombinant Proteins
Substrate Specificity

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10.1042/BJ20040511

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@article{eaf46893a8e5482882286982d1f01e5f,

title = "Human PHOSPHO1 exhibits high specific phosphoethanolamine and phosphocholine phosphatase activities",

abstract = "Human PHOSPHO1 is a phosphatase enzyme for which expression is upregulated in mineralizing cells. This enzyme has been implicated in the generation of P(i) for matrix mineralization, a process central to skeletal development. PHOSPHO1 is a member of the haloacid dehalogenase (HAD) superfamily of Mg2+-dependent hydrolases. However, substrates for PHOSPHO1 are, as yet, unidentified and little is known about its activity. We show here that PHOSPHO1 exhibits high specific activities toward phosphoethanolamine (PEA) and phosphocholine (PCho). Optimal enzymic activity was observed at approx. pH 6.7. The enzyme shows a high specific Mg2+-dependence, with apparent K(m) values of 3.0 microM for PEA and 11.4 microM for PCho. These results provide a novel mechanism for the generation of P(i) in mineralizing cells from PEA and PCho.",

keywords = "Cell Line, Tumor, Ethanolamines, Humans, Metals, Osteosarcoma, Phosphoric Monoester Hydrolases, Phosphorylcholine, Recombinant Proteins, Substrate Specificity",

author = "Roberts, {Scott J} and Stewart, {Alan J} and Sadler, {Peter J} and Colin Farquharson",

year = "2004",

month = aug,

day = "15",

doi = "10.1042/BJ20040511",

language = "English",

volume = "382",

pages = "59--65",

journal = "Biochemical Journal",

issn = "0264-6021",

publisher = "Portland Press Ltd.",

number = "Pt 1",

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TY - JOUR

T1 - Human PHOSPHO1 exhibits high specific phosphoethanolamine and phosphocholine phosphatase activities

AU - Roberts, Scott J

AU - Stewart, Alan J

AU - Sadler, Peter J

AU - Farquharson, Colin

PY - 2004/8/15

Y1 - 2004/8/15

N2 - Human PHOSPHO1 is a phosphatase enzyme for which expression is upregulated in mineralizing cells. This enzyme has been implicated in the generation of P(i) for matrix mineralization, a process central to skeletal development. PHOSPHO1 is a member of the haloacid dehalogenase (HAD) superfamily of Mg2+-dependent hydrolases. However, substrates for PHOSPHO1 are, as yet, unidentified and little is known about its activity. We show here that PHOSPHO1 exhibits high specific activities toward phosphoethanolamine (PEA) and phosphocholine (PCho). Optimal enzymic activity was observed at approx. pH 6.7. The enzyme shows a high specific Mg2+-dependence, with apparent K(m) values of 3.0 microM for PEA and 11.4 microM for PCho. These results provide a novel mechanism for the generation of P(i) in mineralizing cells from PEA and PCho.

AB - Human PHOSPHO1 is a phosphatase enzyme for which expression is upregulated in mineralizing cells. This enzyme has been implicated in the generation of P(i) for matrix mineralization, a process central to skeletal development. PHOSPHO1 is a member of the haloacid dehalogenase (HAD) superfamily of Mg2+-dependent hydrolases. However, substrates for PHOSPHO1 are, as yet, unidentified and little is known about its activity. We show here that PHOSPHO1 exhibits high specific activities toward phosphoethanolamine (PEA) and phosphocholine (PCho). Optimal enzymic activity was observed at approx. pH 6.7. The enzyme shows a high specific Mg2+-dependence, with apparent K(m) values of 3.0 microM for PEA and 11.4 microM for PCho. These results provide a novel mechanism for the generation of P(i) in mineralizing cells from PEA and PCho.

KW - Cell Line, Tumor

KW - Ethanolamines

KW - Humans

KW - Metals

KW - Osteosarcoma

KW - Phosphoric Monoester Hydrolases

KW - Phosphorylcholine

KW - Recombinant Proteins

KW - Substrate Specificity

U2 - 10.1042/BJ20040511

DO - 10.1042/BJ20040511

M3 - Article

C2 - 15175005

SN - 0264-6021

VL - 382

SP - 59

EP - 65

JO - Biochemical Journal

JF - Biochemical Journal

IS - Pt 1

ER -

Human PHOSPHO1 exhibits high specific phosphoethanolamine and phosphocholine phosphatase activities

Abstract / Description of output

Keywords / Materials (for Non-textual outputs)

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