The Chryseobacterium meningosepticum PafA enzyme

Prototype of a new enzyme family of prokaryotic phosphate-irrepressible alkaline phosphatases?

F. Berlutti, C. Passariello, L. Selan, M. C. Thaller, G. M. Rossolini

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Chryseobacterium meningosepticum is an aerobic Gram-negative rod widely distributed in natural environments. Unlike many bacteria, it produces a phosphate-irrepressible periplasmic alkaline phosphatase (AP). This work describes cloning of the gene encoding that enzyme from C. meningosepticum CCUG 4310 (NCTC 10585), and preliminary characterization of its product. The gene, named pafA, encodes a protein (PafA) of 546 amino acids with a calculated molecular mass of the mature peptide of 58682 Da. PafA exhibits high sequence identity with the PhoV AP of Synechococcus PCC 7942 (49.9% identity) and with the Cda Ca2+-dependent ATPase of Myroides odoratus (51.9% identity), while being more distantly related to the PhoD AP of Zymomonas mobilis (22.1% identity) and to the PhoA AP of Escherichia coli (14.0% identity). PafA was partially purified; it exhibits optimal activity at pH 8.5 and is active towards a broad spectrum of substrates including both phosphomonoesters and ATP, with preferential activity for the latter compound. The present findings allow definition of a new family of APs including 60 kDa, periplasmic enzymes whose expression is not influenced by freely available Pi in the medium. Moreover, PafA can be considered an evolutionary intermediate between Ca2+-ATPase of M. odoratus and the APs PhoV of Synechococcus PCC 7942 and PhoD of Z. mobilis.

Original languageEnglish
Pages (from-to)2831-2839
Number of pages9
JournalMicrobiology
Volume147
Issue number10
Publication statusPublished - 2001

Fingerprint

Chryseobacterium
Alkaline Phosphatase
Phosphates
Zymomonas
Synechococcus
Calcium-Transporting ATPases
Enzymes
Genes
Organism Cloning
Adenosine Triphosphate
Escherichia coli
Bacteria
Amino Acids
Peptides
Chryseobacterium meningosepticum periplasmic alkaline phosphatase
Proteins

Keywords

  • Ca-dependent ATPase
  • Cda
  • Flavobacteria
  • PhoD
  • PhoV

ASJC Scopus subject areas

  • Microbiology

Cite this

Berlutti, F., Passariello, C., Selan, L., Thaller, M. C., & Rossolini, G. M. (2001). The Chryseobacterium meningosepticum PafA enzyme: Prototype of a new enzyme family of prokaryotic phosphate-irrepressible alkaline phosphatases? Microbiology, 147(10), 2831-2839.

The Chryseobacterium meningosepticum PafA enzyme : Prototype of a new enzyme family of prokaryotic phosphate-irrepressible alkaline phosphatases? / Berlutti, F.; Passariello, C.; Selan, L.; Thaller, M. C.; Rossolini, G. M.

In: Microbiology, Vol. 147, No. 10, 2001, p. 2831-2839.

Research output: Contribution to journalArticle

Berlutti, F, Passariello, C, Selan, L, Thaller, MC & Rossolini, GM 2001, 'The Chryseobacterium meningosepticum PafA enzyme: Prototype of a new enzyme family of prokaryotic phosphate-irrepressible alkaline phosphatases?', Microbiology, vol. 147, no. 10, pp. 2831-2839.
Berlutti, F. ; Passariello, C. ; Selan, L. ; Thaller, M. C. ; Rossolini, G. M. / The Chryseobacterium meningosepticum PafA enzyme : Prototype of a new enzyme family of prokaryotic phosphate-irrepressible alkaline phosphatases?. In: Microbiology. 2001 ; Vol. 147, No. 10. pp. 2831-2839.
@article{d690c8defa87402086771a00f2695c27,
title = "The Chryseobacterium meningosepticum PafA enzyme: Prototype of a new enzyme family of prokaryotic phosphate-irrepressible alkaline phosphatases?",
abstract = "Chryseobacterium meningosepticum is an aerobic Gram-negative rod widely distributed in natural environments. Unlike many bacteria, it produces a phosphate-irrepressible periplasmic alkaline phosphatase (AP). This work describes cloning of the gene encoding that enzyme from C. meningosepticum CCUG 4310 (NCTC 10585), and preliminary characterization of its product. The gene, named pafA, encodes a protein (PafA) of 546 amino acids with a calculated molecular mass of the mature peptide of 58682 Da. PafA exhibits high sequence identity with the PhoV AP of Synechococcus PCC 7942 (49.9{\%} identity) and with the Cda Ca2+-dependent ATPase of Myroides odoratus (51.9{\%} identity), while being more distantly related to the PhoD AP of Zymomonas mobilis (22.1{\%} identity) and to the PhoA AP of Escherichia coli (14.0{\%} identity). PafA was partially purified; it exhibits optimal activity at pH 8.5 and is active towards a broad spectrum of substrates including both phosphomonoesters and ATP, with preferential activity for the latter compound. The present findings allow definition of a new family of APs including 60 kDa, periplasmic enzymes whose expression is not influenced by freely available Pi in the medium. Moreover, PafA can be considered an evolutionary intermediate between Ca2+-ATPase of M. odoratus and the APs PhoV of Synechococcus PCC 7942 and PhoD of Z. mobilis.",
keywords = "Ca-dependent ATPase, Cda, Flavobacteria, PhoD, PhoV",
author = "F. Berlutti and C. Passariello and L. Selan and Thaller, {M. C.} and Rossolini, {G. M.}",
year = "2001",
language = "English",
volume = "147",
pages = "2831--2839",
journal = "Microbiology",
issn = "1350-0872",
publisher = "Society for General Microbiology",
number = "10",

}

TY - JOUR

T1 - The Chryseobacterium meningosepticum PafA enzyme

T2 - Prototype of a new enzyme family of prokaryotic phosphate-irrepressible alkaline phosphatases?

AU - Berlutti, F.

AU - Passariello, C.

AU - Selan, L.

AU - Thaller, M. C.

AU - Rossolini, G. M.

PY - 2001

Y1 - 2001

N2 - Chryseobacterium meningosepticum is an aerobic Gram-negative rod widely distributed in natural environments. Unlike many bacteria, it produces a phosphate-irrepressible periplasmic alkaline phosphatase (AP). This work describes cloning of the gene encoding that enzyme from C. meningosepticum CCUG 4310 (NCTC 10585), and preliminary characterization of its product. The gene, named pafA, encodes a protein (PafA) of 546 amino acids with a calculated molecular mass of the mature peptide of 58682 Da. PafA exhibits high sequence identity with the PhoV AP of Synechococcus PCC 7942 (49.9% identity) and with the Cda Ca2+-dependent ATPase of Myroides odoratus (51.9% identity), while being more distantly related to the PhoD AP of Zymomonas mobilis (22.1% identity) and to the PhoA AP of Escherichia coli (14.0% identity). PafA was partially purified; it exhibits optimal activity at pH 8.5 and is active towards a broad spectrum of substrates including both phosphomonoesters and ATP, with preferential activity for the latter compound. The present findings allow definition of a new family of APs including 60 kDa, periplasmic enzymes whose expression is not influenced by freely available Pi in the medium. Moreover, PafA can be considered an evolutionary intermediate between Ca2+-ATPase of M. odoratus and the APs PhoV of Synechococcus PCC 7942 and PhoD of Z. mobilis.

AB - Chryseobacterium meningosepticum is an aerobic Gram-negative rod widely distributed in natural environments. Unlike many bacteria, it produces a phosphate-irrepressible periplasmic alkaline phosphatase (AP). This work describes cloning of the gene encoding that enzyme from C. meningosepticum CCUG 4310 (NCTC 10585), and preliminary characterization of its product. The gene, named pafA, encodes a protein (PafA) of 546 amino acids with a calculated molecular mass of the mature peptide of 58682 Da. PafA exhibits high sequence identity with the PhoV AP of Synechococcus PCC 7942 (49.9% identity) and with the Cda Ca2+-dependent ATPase of Myroides odoratus (51.9% identity), while being more distantly related to the PhoD AP of Zymomonas mobilis (22.1% identity) and to the PhoA AP of Escherichia coli (14.0% identity). PafA was partially purified; it exhibits optimal activity at pH 8.5 and is active towards a broad spectrum of substrates including both phosphomonoesters and ATP, with preferential activity for the latter compound. The present findings allow definition of a new family of APs including 60 kDa, periplasmic enzymes whose expression is not influenced by freely available Pi in the medium. Moreover, PafA can be considered an evolutionary intermediate between Ca2+-ATPase of M. odoratus and the APs PhoV of Synechococcus PCC 7942 and PhoD of Z. mobilis.

KW - Ca-dependent ATPase

KW - Cda

KW - Flavobacteria

KW - PhoD

KW - PhoV

UR - http://www.scopus.com/inward/record.url?scp=0034775185&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034775185&partnerID=8YFLogxK

M3 - Article

VL - 147

SP - 2831

EP - 2839

JO - Microbiology

JF - Microbiology

SN - 1350-0872

IS - 10

ER -