Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family.

Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family. Abstract Text:

Ekaterina Kuznetsova,Michael Proudfoot,Claudio F Gonzalez,Greg Brown,Marina V Omelchenko,Ivan Borozan,Liran Carmel,Yuri I Wolf,Hirotada Mori,Alexei V Savchenko,Cheryl H Arrowsmith,Eugene V Koonin,Aled M Edwards,Alexander F Yakunin,

Haloacid dehalogenase (HAD)-like hydrolases are a vast superfamily of largely uncharacterized enzymes, with a few members shown to possess phosphatase, beta-phosphoglucomutase, phosphonatase, and dehalogenase activities. Using a representative set of 80 phosphorylated substrates, we characterized the substrate specificities of 23 soluble HADs encoded in the Escherichia coli genome. We identified small molecule phosphatase activity in 21 HADs and beta-phosphoglucomutase activity in one protein. The E. coli HAD phosphatases show high catalytic efficiency and affinity to a wide range of phosphorylated metabolites that are intermediates of various metabolic reactions. Rather than following the classical "one enzyme-one substrate" model, most of the E. coli HADs show remarkably broad and overlapping substrate spectra. At least 12 reactions catalyzed by HADs currently have no EC numbers assigned in Enzyme Nomenclature. Surprisingly, most HADs hydrolyzed small phosphodonors (acetyl phosphate, carbamoyl phosphate, and phosphoramidate), which also serve as substrates for autophosphorylation of the receiver domains of the two-component signal transduction systems. The physiological relevance of the phosphatase activity with the preferred substrate was validated in vivo for one of the HADs, YniC. Many of the secondary activities of HADs might have no immediate physiological function but could comprise a reservoir for evolution of novel phosphatases.

Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family. Publishing Authors By Initials

E Kuznetsova,M Proudfoot,CF Gonzalez,G Brown,MV Omelchenko,I Borozan,L Carmel,YI Wolf,H Mori,AV Savchenko,CH Arrowsmith,EV Koonin,AM Edwards,AF Yakunin,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research

PUBMED ID PMID:

MEDLINE DATE:

Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: The Journal of biological chemistry

VOLUME: 281

Page Numbers: 36149-61

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 21

MONTH: 09

YEAR: 2006

Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985121

Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family. Keywords Mesh Terms:

KEYWORDS: Substrate Specificity

MESH TERMS: genetics

Chemical & Substance for Abstract: Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family. Information

Substance Name: Phosphoric Monoester Hydrolases

Registry Number: EC 3.1.3.-

Grant and Affiliation Information for Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family.

AFFILIATION: Banting and Best Department of Medical Research, University of Toronto, Toronto, Ontario, Canada.

Country: United States

AGENCY: United States NIGMS

GRANT: GM62414-01

ACRONYM: GM

MEDLINETA: J Biol Chem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family Related Publications

• A Novel Family of Sequence-specific Endoribonucleases Associated with the Clustered Regularly Interspaced Short Palindromic Repeats.
• Biochemical and structural characterization of a novel family of cystathionine beta-synthase domain proteins fused to a Zn ribbon-like domain.
• Functional and Structural Characterization of Four Glutaminases from Escherichia coli and Bacillus subtilis.
• Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family.
• High throughput screening of purified proteins for enzymatic activity.
• Molecular basis of the antimutagenic activity of the house-cleaning inosine triphosphate pyrophosphatase RdgB from Escherichia coli.