Biochemical characterization of an active pyrophosphate-dependent phosphofructokinase from Treponema pallidum

Russell S. Roberson; Ron S. Ronimus; Susanne Gephard; Hugh W. Morgan

doi:10.1016/S0378-1097(00)00518-8

Biochemical characterization of an active pyrophosphate-dependent phosphofructokinase from Treponema pallidum

Russell S. Roberson, Ron S. Ronimus, Susanne Gephard, Hugh W. Morgan

Anesthesiology & Pain Management

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

8 Scopus citations

Abstract

An active pyrophosphate-dependent phosphofructokinase containing a six residue polyhistidine tag has been cloned from Treponema pallidum, and characterized biochemically. The phosphofructokinase has pH optima for activity of 8.0 for both the forward and reverse reactions. The apparent K_m for pyrophosphate was 0.042 mM (V_max of 141 U mg^-1 protein) and for fructose-6-phosphate, 0.529 mM. The apparent K_m for the reverse reaction for fructose-1,6-diphosphate was 0.267 mM (V_max of 42.4 U mg^-1 protein). The enzyme appears to be both a dimer and non-allosteric.

Original language	English (US)
Pages (from-to)	257-260
Number of pages	4
Journal	FEMS Microbiology Letters
Volume	194
Issue number	2
DOIs	https://doi.org/10.1016/S0378-1097(00)00518-8
State	Published - Jan 15 2001

Keywords

Glycolysis
Phosphofructokinase
Pyrophosphate
Syphilis
Treponema pallidum

ASJC Scopus subject areas

Microbiology
Molecular Biology
Genetics

Access to Document

10.1016/S0378-1097(00)00518-8

Cite this

@article{4dc8e0536eed4f41b7c4dd9b7e7efaeb,

title = "Biochemical characterization of an active pyrophosphate-dependent phosphofructokinase from Treponema pallidum",

abstract = "An active pyrophosphate-dependent phosphofructokinase containing a six residue polyhistidine tag has been cloned from Treponema pallidum, and characterized biochemically. The phosphofructokinase has pH optima for activity of 8.0 for both the forward and reverse reactions. The apparent Km for pyrophosphate was 0.042 mM (Vmax of 141 U mg-1 protein) and for fructose-6-phosphate, 0.529 mM. The apparent Km for the reverse reaction for fructose-1,6-diphosphate was 0.267 mM (Vmax of 42.4 U mg-1 protein). The enzyme appears to be both a dimer and non-allosteric.",

keywords = "Glycolysis, Phosphofructokinase, Pyrophosphate, Syphilis, Treponema pallidum",

author = "Roberson, {Russell S.} and Ronimus, {Ron S.} and Susanne Gephard and Morgan, {Hugh W.}",

year = "2001",

month = jan,

day = "15",

doi = "10.1016/S0378-1097(00)00518-8",

language = "English (US)",

volume = "194",

pages = "257--260",

journal = "FEMS Microbiology Letters",

issn = "0378-1097",

publisher = "Wiley-Blackwell",

number = "2",

}

TY - JOUR

T1 - Biochemical characterization of an active pyrophosphate-dependent phosphofructokinase from Treponema pallidum

AU - Roberson, Russell S.

AU - Ronimus, Ron S.

AU - Gephard, Susanne

AU - Morgan, Hugh W.

PY - 2001/1/15

Y1 - 2001/1/15

N2 - An active pyrophosphate-dependent phosphofructokinase containing a six residue polyhistidine tag has been cloned from Treponema pallidum, and characterized biochemically. The phosphofructokinase has pH optima for activity of 8.0 for both the forward and reverse reactions. The apparent Km for pyrophosphate was 0.042 mM (Vmax of 141 U mg-1 protein) and for fructose-6-phosphate, 0.529 mM. The apparent Km for the reverse reaction for fructose-1,6-diphosphate was 0.267 mM (Vmax of 42.4 U mg-1 protein). The enzyme appears to be both a dimer and non-allosteric.

AB - An active pyrophosphate-dependent phosphofructokinase containing a six residue polyhistidine tag has been cloned from Treponema pallidum, and characterized biochemically. The phosphofructokinase has pH optima for activity of 8.0 for both the forward and reverse reactions. The apparent Km for pyrophosphate was 0.042 mM (Vmax of 141 U mg-1 protein) and for fructose-6-phosphate, 0.529 mM. The apparent Km for the reverse reaction for fructose-1,6-diphosphate was 0.267 mM (Vmax of 42.4 U mg-1 protein). The enzyme appears to be both a dimer and non-allosteric.

KW - Glycolysis

KW - Phosphofructokinase

KW - Pyrophosphate

KW - Syphilis

KW - Treponema pallidum

UR - http://www.scopus.com/inward/record.url?scp=0035862448&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035862448&partnerID=8YFLogxK

U2 - 10.1016/S0378-1097(00)00518-8

DO - 10.1016/S0378-1097(00)00518-8

M3 - Article

C2 - 11164318

AN - SCOPUS:0035862448

SN - 0378-1097

VL - 194

SP - 257

EP - 260

JO - FEMS Microbiology Letters

JF - FEMS Microbiology Letters

IS - 2

ER -

Biochemical characterization of an active pyrophosphate-dependent phosphofructokinase from Treponema pallidum

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this