Rhea - reaction knowledgebase

Enzymes

UniProtKB ^help_outline	1,237 proteins
Enzyme class ^help_outline	EC 2.7.1.207 protein-N(pi)-phosphohistidine--lactose phosphotransferase

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Name ^help_outline lactose Identifier CHEBI:17716 (CAS: 63-42-3) ^help_outline Charge 0 Formula C12H22O11 InChIKey^help_outline GUBGYTABKSRVRQ-QKKXKWKRSA-N SMILES^help_outline OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 11 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name^help_outline N^π-phospho-L-histidyl-[protein] Identifier RHEA-COMP:9746 Reactive part ^help_outline
- Name ^help_outline N^π-phospho-L-histidine residue Identifier CHEBI:64837 Charge -2 Formula C6H6N3O4P SMILES^help_outline C(*)(=O)[C@@H](N*)CC=1N(C=NC1)P([O-])(=O)[O-] 2D coordinates Mol file for the small molecule Search links Involved in 24 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Search links Involved in 24 reaction(s) Find proteins in UniProtKB for this molecule
Name ^help_outline lactose 6-phosphate Identifier CHEBI:79080 Charge -2 Formula C12H21O14P InChIKey^help_outline ITPHOIFCAFNCLL-QKKXKWKRSA-L SMILES^help_outline OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O[C@@H]1O[C@H](COP([O-])([O-])=O)[C@H](O)[C@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name^help_outline L-histidyl-[protein] Identifier RHEA-COMP:9745 Reactive part ^help_outline
- Name ^help_outline L-histidine residue Identifier CHEBI:29979 Charge 0 Formula C6H7N3O SMILES^help_outline C(*)(=O)[C@@H](N*)CC=1N=CNC1 2D coordinates Mol file for the small molecule Search links Involved in 40 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Search links Involved in 32 reaction(s) Find proteins in UniProtKB for this molecule

Cross-references

	RHEA:42400	RHEA:42401	RHEA:42402	RHEA:42403
Reaction direction	undefined	left-to-right	right-to-left	bidirectional
UniProtKB ^help_outline	1,237 proteins
EC numbers ^help_outline	2.7.1.207
KEGG ^help_outline				R04393
MetaCyc ^help_outline		RXN-15085

Publications

Characterization of the lactose-specific enzymes of the phosphotransferase system in Lactococcus lactis.

de Vos W.M., Boerrigter I.J., van Rooyen R.J., Reiche B., Hengstenberg W.

The plasmid-encoded lactose genes of the Lactococcus lactis phosphotransferase system encoding Enzyme IIIlac (lacF) and Enzyme IIlac (lacE) have been identified and cloned in Escherichia coli and L. lactis. Nucleotide sequence and transcription analysis showed that these genes are organized into a ... >> More

The plasmid-encoded lactose genes of the Lactococcus lactis phosphotransferase system encoding Enzyme IIIlac (lacF) and Enzyme IIlac (lacE) have been identified and cloned in Escherichia coli and L. lactis. Nucleotide sequence and transcription analysis showed that these genes are organized into a lactose-inducible operon with the gene order lacF-lacE-lacG-lacX, the latter two genes encoding phospho-beta-galactosidase and a 34-kDa protein with an unknown function, respectively. The lac-operon is immediately followed by an IS element that is homologous to ISS1. Enzyme IIIlac was purified from L. lactis and determination of its NH2-terminal sequence demonstrated that the lacF gene starts with a TTG codon and encodes a 105 amino acid protein (Mr = 11416). Cross-linking studies with the purified enzyme showed that Enzyme IIIlac is active as a trimer. A mutant lacF gene was identified in strain YP2-5 and appeared to encode Enzyme IIIlac containing the missense mutation G18E. The lacF gene could be expressed under control of vector-located promoter sequences resulting in overproduction of Enzyme IIIlac in E. coli and complementation of the L. lactis lacF mutant YP2-5. The deduced amino acid sequence of Enzyme IIlac consists of 586 amino acids (Mr = 61562) and shows the characteristics of a hydrophobic, integral membrane protein. The deduced primary structures of the L. lactis Enzyme IIIlac and Enzyme IIlac are homologous to those of Staphylococcus aureus (72 and 71% identity, respectively) and Lactobacillus casei (48 and 47% identity, respectively). In contrast, the organization of the lactose genes differs significantly between those Gram-positive bacteria. Heterogramic homology in specific domains was observed between the derived amino acid sequences of the lactose-specific enzymes and that of E. coli Enzyme IIIcel and Enzyme IIcel, which suggest a common function in the transport and phosphorylation of these structurally related beta-glucosides. << Less

J. Biol. Chem. 265:22554-22560(1990) [PubMed] [EuropePMC]
Solubilization of the membrane bound lactose specific component of the staphylococcal PEP dependant phosphotransferase system.

Hengstenberg W.

The membrane bound lactose specific component of the PEP dependant phosphotransferase system of Staphylococcus aureus has been solubilized using the non ionic detergent Triton X-100. Some properties of the crude soluble enzyme are reported.

FEBS Lett. 8:277-280(1970) [PubMed] [EuropePMC]
Lactose-specific enzyme II of the phosphoenolpyruvate-dependent phosphotransferase system of Staphylococcus aureus. Purification of the histidine-tagged transmembrane component IICBLac and its hydrophilic IIB domain by metal-affinity chromatography, and functional characterization.

Peters D., Frank R., Hengstenberg W.

The lactose-specific integral-membrane-protein enzyme II (IICBLac) of the bacterial phosphoenolpyruvate-dependent phosphotransferase system of Staphylococcus aureus catalyses the uptake and phosphorylation of lactose. It consists of an N-terminal membrane-spanning IIC domain and a C-terminal hydro ... >> More

The lactose-specific integral-membrane-protein enzyme II (IICBLac) of the bacterial phosphoenolpyruvate-dependent phosphotransferase system of Staphylococcus aureus catalyses the uptake and phosphorylation of lactose. It consists of an N-terminal membrane-spanning IIC domain and a C-terminal hydrophilic IIB domain. IICBLac was fused with a C-terminal tag of six histidine residues using recombinant DNA technology. The resulting protein, IICBLac-His, was produced in Escherichia coli and purified under nondenaturing conditions to homogenity. The purification procedure consists of a NaOH extraction step followed by solubilisation with Triton X-100, and metal-affinity chromatography using Ni(2+)-nitrilotriacetic acid resin. The purified recombinant His-tagged protein possessed substrate specificity identical to that of the wild-type protein. To investigate the hydrophilic IIB domain, the DNA sequence coding for IIB and the His tag were fused in-frame to a DNA sequence specific for an initiation signal. The overproduced recombinant IIBLac-His was obtained by metal-affinity chromatography in pure form. Bacterial phosphotransferase-system-dependent phosphorylation of IIB-His was demonstrated in a photometric assay and by urea/polyacrylamide gel electrophoresis. The phosphorylation activity of the mutant protein [C476S]-IICBLac, containing the mutagenized phosphorylation site, was restored in the presence of IIBLac-His in a phosphorylation assay. << Less

Eur. J. Biochem. 228:798-804(1995) [PubMed] [EuropePMC]
Identification of the genes for the lactose-specific components of the phosphotransferase system in the lac operon of Staphylococcus aureus.

Breidt F. Jr., Hengstenberg W., Finkeldei U., Stewart G.C.

The nucleotide and deduced amino acid sequences of the lacE and lacF genes, which code for the lactose-specific Enzyme II and Enzyme III of the Staphylococcus aureus phosphotransferase system, are presented. The primary translation products consist of a hydrophobic protein of 572 amino acids (Mr = ... >> More

The nucleotide and deduced amino acid sequences of the lacE and lacF genes, which code for the lactose-specific Enzyme II and Enzyme III of the Staphylococcus aureus phosphotransferase system, are presented. The primary translation products consist of a hydrophobic protein of 572 amino acids (Mr = 62,688) and a polypeptide of 103 amino acids (Mr = 11,372), respectively. The assignment of lacF as the gene for Enzyme IIIlac was based upon the known amino acid sequence of the protein. The identity of lacE as encoding Enzyme IIlac was based upon immunoreactivity of the cloned gene product with antibodies raised against purified Enzyme IIlac from S. aureus and an assay of biological function of the protein expressed in Escherichia coli. The order of the known genes of the S. aureus lac operon is lacF-lacE-lacG, the latter encoding phospho-beta-galactosidase. << Less

J. Biol. Chem. 262:16444-16449(1987) [PubMed] [EuropePMC]
Lactose transport in Streptococcus mutans: isolation and characterization of factor IIIlac, a specific protein component of the phosphoenolpyruvate-lactose phosphotransferase system.

Vadeboncoeur C., Proulx M.

The transport of lactose in Streptococcus mutans is mediated via an inducible phosphoenolpyruvate-lactose phosphotransferase system. This system requires for catalytic activity a membrane fraction (enzyme II), two general proteins called enzyme I and HPr, and a soluble specific protein termed fact ... >> More

The transport of lactose in Streptococcus mutans is mediated via an inducible phosphoenolpyruvate-lactose phosphotransferase system. This system requires for catalytic activity a membrane fraction (enzyme II), two general proteins called enzyme I and HPr, and a soluble specific protein termed factor IIIlac. This protein factor was purified from S. mutans ATCC 27352 by chromatographies on DEAE-cellulose, hydroxylapatite, Ultrogel AcA 34, and phosphocellulose. The purified protein migrated as a single band with a molecular weight of 10,000 on polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate and urea. The molecular weight calculated from the amino acid composition was 10,541. Gel filtration of the native protein gave a molecular weight of 41,500. Its isoelectric point was ca. 4.70. A specific antiserum was prepared against purified factor IIIlac. Immunodiffusion experiments revealed that only cellular extracts from lactose-grown cells contained factor IIIlac. A cross-reaction was observed with all of the S. mutans strains tested as well as with Streptococcus sanguis 10556, Streptococcus lactis 11454, and Staphylococcus aureus 6538. No precipitin band was observed with extracts of Streptococcus salivarius, Streptococcus faecalis, Lactobacillus casei, and Bacillus subtilis. << Less

Infect. Immun. 46:213-219(1984) [PubMed] [EuropePMC]

RHEA:42400 lactose(out) + N(pros)-phospho-L-histidyl-[protein] = lactose 6-phosphate(in) + L-histidyl-[protein]

Enzymes

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Cross-references

Publications

Characterization of the lactose-specific enzymes of the phosphotransferase system in Lactococcus lactis.

Solubilization of the membrane bound lactose specific component of the staphylococcal PEP dependant phosphotransferase system.

Lactose-specific enzyme II of the phosphoenolpyruvate-dependent phosphotransferase system of Staphylococcus aureus. Purification of the histidine-tagged transmembrane component IICBLac and its hydrophilic IIB domain by metal-affinity chromatography, and functional characterization.

Identification of the genes for the lactose-specific components of the phosphotransferase system in the lac operon of Staphylococcus aureus.

Lactose transport in Streptococcus mutans: isolation and characterization of factor IIIlac, a specific protein component of the phosphoenolpyruvate-lactose phosphotransferase system.