Rhea - reaction knowledgebase

Enzymes

UniProtKB ^help_outline	5 proteins
Enzyme class ^help_outline	EC 3.1.3.10 glucose-1-phosphatase
GO Molecular Function ^help_outline	GO:0008877 glucose-1-phosphatase activity

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Name ^help_outline α-D-glucose 1-phosphate Identifier CHEBI:58601 Charge -2 Formula C6H11O9P InChIKey^help_outline HXXFSFRBOHSIMQ-VFUOTHLCSA-L SMILES^help_outline OC[C@H]1O[C@H](OP([O-])([O-])=O)[C@H](O)[C@@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 41 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline H₂O Identifier CHEBI:15377 (CAS: 7732-18-5) ^help_outline Charge 0 Formula H2O InChIKey^help_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILES^help_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,264 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline D-glucose Identifier CHEBI:4167 (CAS: 2280-44-6) ^help_outline Charge 0 Formula C6H12O6 InChIKey^help_outline WQZGKKKJIJFFOK-GASJEMHNSA-N SMILES^help_outline OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 162 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline phosphate Identifier CHEBI:43474 Charge -2 Formula HO4P InChIKey^help_outline NBIIXXVUZAFLBC-UHFFFAOYSA-L SMILES^help_outline OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1,002 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule

Cross-references

	RHEA:19933	RHEA:19934	RHEA:19935	RHEA:19936
Reaction direction	undefined	left-to-right	right-to-left	bidirectional
UniProtKB ^help_outline	5 proteins
EC numbers ^help_outline	3.1.3.10
Gene Ontology ^help_outline	GO:0008877
KEGG ^help_outline				R00304
MetaCyc ^help_outline		GLUCOSE-1-PHOSPHAT-RXN
EcoCyc ^help_outline		GLUCOSE-1-PHOSPHAT-RXN

Publications

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

Kuznetsova E., Proudfoot M., Gonzalez C.F., Brown G., Omelchenko M.V., Borozan I., Carmel L., Wolf Y.I., Mori H., Savchenko A.V., Arrowsmith C.H., Koonin E.V., Edwards A.M., Yakunin A.F.

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 ... >> More

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. << Less

J. Biol. Chem. 281:36149-36161(2006) [PubMed] [EuropePMC]

This publication is cited by 7 other entries.
A hexose-1-phosphatase in silkworm blood.

FAULKNER P.

Biochem J 60:590-596(1955) [PubMed] [EuropePMC]
Yihx-encoded haloacid dehalogenase-like phosphatase HAD4 from Escherichia coli is a specific alpha-d-glucose 1-phosphate hydrolase useful for substrate-selective sugar phosphate transformations.

Pfeiffer M., Wildberger P., Nidetzky B.

Phosphomonoester hydrolases (phosphatases; EC 3.1.3.) often exhibit extremely relaxed substrate specificity which limits their application to substrate-selective biotransformations. In search of a phosphatase catalyst specific for hydrolyzing α-d-glucose 1-phosphate (αGlc 1-P), we selected ... >> More

Phosphomonoester hydrolases (phosphatases; EC 3.1.3.) often exhibit extremely relaxed substrate specificity which limits their application to substrate-selective biotransformations. In search of a phosphatase catalyst specific for hydrolyzing α-d-glucose 1-phosphate (αGlc 1-P), we selected haloacid dehalogenase-like phosphatase 4 (HAD4) from Escherichia coli and obtained highly active recombinant enzyme through a fusion protein (Zbasic2_HAD4) that contained Zbasic2, a strongly positively charged three α-helical bundle module, at its N-terminus. Highly pure Zbasic2_HAD4 was prepared directly from E. coli cell extract using capture and polishing combined in a single step of cation exchange chromatography. Kinetic studies showed Zbasic2_HAD4 to exhibit 565-fold preference for hydrolyzing αGlc 1-P (kcat/KM = 1.87 ± 0.03 mM-1 s-1; 37 °C, pH 7.0) as compared to d-glucose 6-phosphate (Glc 6-P). Also among other sugar phosphates, αGlc 1-P was clearly preferred. Using different mixtures of αGlc 1-P and Glc 6-P (e.g. 180 mM each) as the substrate, Zbasic2_HAD4 could be used to selectively convert the αGlc 1-P present, leaving back all of the Glc 6-P for recovery. Zbasic2_HAD4 was immobilized conveniently using direct loading of E. coli cell extract on sulfonic acid group-containing porous carriers, yielding a recyclable heterogeneous biocatalyst that was nearly as effective as the soluble enzyme, probably because protein attachment to the anionic surface occurred in a preferred orientation via the cationic Zbasic2 module. Selective removal of αGlc 1-P from sugar phosphate preparations could be an interesting application of Zbasic2_HAD4 for which readily available broad-spectrum phosphatases are unsuitable. << Less

J. Mol. Catal., B Enzym. 110:39-46(2014) [PubMed] [EuropePMC]
The hydrolysis of glucose monophosphates by a phosphatase preparation from pea seeds.

TURNER D.H., TURNER J.F.

Biochem J 74:486-491(1960) [PubMed] [EuropePMC]

RHEA:19933 alpha-D-glucose 1-phosphate + H2O = D-glucose + phosphate

Enzymes

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Cross-references

Publications

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

A hexose-1-phosphatase in silkworm blood.

Yihx-encoded haloacid dehalogenase-like phosphatase HAD4 from Escherichia coli is a specific alpha-d-glucose 1-phosphate hydrolase useful for substrate-selective sugar phosphate transformations.

The hydrolysis of glucose monophosphates by a phosphatase preparation from pea seeds.