lacZ beta-galactosidase [Escherichia coli str. K-12 substr. MG1655] - Gene

Summary

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Official Symbol: lacZ
Official Full Name: beta-galactosidase
Primary source: ECOCYC:EG10527
Locus tag: b0344
See related: ASAP:ABE-0001183
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage: Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as: ECK0341
Summary: Repressed during biofilm formation. [More information is available at EcoGene: EG10527]. galacotsidase is a metalloenzyme exhibiting broad substrate specificity. [More information is available at EcoCyc: EG10527].
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Genomic context

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Sequence:: NC_000913.3 (363231..366305, complement)

NC_000913.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

this study reports the structure of a complex between Escherichia coli beta-galactosidase and the cell-permeant inhibitor phenylethyl beta-D-thiogalactopyranoside, determined by cryo-EM at an average resolution of ~2.2 angstroms.
Title: 2.2 Å resolution cryo-EM structure of β-galactosidase in complex with a cell-permeant inhibitor.
Report the solution structure at approximately 3.2-A resolution by using single-particle cryo-electron microscopy (cryo-EM). Densities for most side chains, including those of residues in the active site, and a catalytic Mg(2+) ion can be discerned.
Title: Structure of β-galactosidase at 3.2-Å resolution obtained by cryo-electron microscopy.
Results on lar, a lac promoter variant indicate the increase as well as the decrease in RNA production with increasing Mg2+ concentration; these changes are, at least partially, caused by changes in the dynamics of formation of the open complex, during transciption initiation.
Title: Effects of Mg(2+) on in vivo transcriptional dynamics of the lar promoter.
study demonstrate an enhancement of beta-galactosidase activity when the enzyme is produced in an oxidizing environment and, consequently, the formation of a disulfide bond in E. coli beta-galactosidase under these conditions
Title: Disulfide bond formation and activation of Escherichia coli β-galactosidase under oxidizing conditions.
Substrate affinity to N460D-beta-galactosidase was enhanced through greater binding enthalpy (stronger H-bonds through the bridging water) while better affinity to N460T-beta-galactosidase occurred because of greater binding entropy.
Title: Substitution for Asn460 cripples β-galactosidase (Escherichia coli) by increasing substrate affinity and decreasing transition state stability.
the hydrophobic and H-bonding properties of Ser-796 result in interactions strong enough to stabilize the open or closed conformations of the loop but weak enough to allow loop movement during the reaction
Title: Ser-796 of β-galactosidase (Escherichia coli) plays a key role in maintaining a balance between the opened and closed conformations of the catalytically important active site loop.
Studies reengineered reporters that detect specific base substitutions or frameshifts in lacZ with the reverting lacZ locus on the chromosome rather than an F' element.
Title: Insights into mutagenesis using Escherichia coli chromosomal lacZ strains that enable detection of a wide spectrum of mutational events.
Arg-599 of b-galactosidase of Escherichia coli is important as an anchor for the open conformations of Phe-601 and the active-site loop.
Title: Importance of Arg-599 of β-galactosidase (Escherichia coli) as an anchor for the open conformations of Phe-601 and the active-site loop.
The active site Mg(2+) is not necessary for LacZ structure and is important for mediating the interactions between the active site components.
Title: Studies of Glu-416 variants of beta-galactosidase (E. coli) show that the active site Mg(2+) is not important for structure and indicate that the main role of Mg (2+) is to mediate optimization of active site chemistry.
The results indicate that His-418, together with the Mg(2+), modulate the central role of Glu-461 in binding and as a general acid/base catalyst in the overall catalytic mechanism.
Title: Direct and indirect roles of His-418 in metal binding and in the activity of beta-galactosidase (E. coli).

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Pathways from PubChem

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by EcoCyc

Function	Evidence Code	Pubs
enables alkali metal ion binding	IDA Inferred from Direct Assay more info	PubMed
enables beta-galactosidase activity	IBA Inferred from Biological aspect of Ancestor more info
enables beta-galactosidase activity	IDA Inferred from Direct Assay more info	PubMed
enables beta-galactosidase activity	IEA Inferred from Electronic Annotation more info
enables carbohydrate binding	IEA Inferred from Electronic Annotation more info
enables hydrolase activity, acting on glycosyl bonds	IEA Inferred from Electronic Annotation more info
enables identical protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables magnesium ion binding	IDA Inferred from Direct Assay more info	PubMed
enables magnesium ion binding	IEA Inferred from Electronic Annotation more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in carbohydrate metabolic process	IEA Inferred from Electronic Annotation more info
involved_in catabolic process	IEA Inferred from Electronic Annotation more info
involved_in lactose catabolic process	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within lactose catabolic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in lactose catabolic process	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
part_of beta-galactosidase complex	IBA Inferred from Biological aspect of Ancestor more info
part_of beta-galactosidase complex	IDA Inferred from Direct Assay more info	PubMed
part_of beta-galactosidase complex	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: beta-galactosidase

NP_414878.1

EC 3.2.1.108

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_000913.3 Reference assembly

Range

363231..366305 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NP_414878.1 beta-galactosidase [Escherichia coli str. K-12 substr. MG1655]

See identical proteins and their annotated locations for NP_414878.1

Status: PROVISIONAL

UniProtKB/TrEMBL

A0A376X5J4, A0AAI9MEL2

Conserved Domains (1) summary

PRK09525
Location:1 → 1024

lacZ; beta-galactosidase