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    ggt glutathione hydrolase proenzyme [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 947947, updated on 17-Dec-2024

    Summary

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    Official Symbol
    ggt
    Official Full Name
    glutathione hydrolase proenzyme
    Primary source
    ECOCYC:EG10374
    Locus tag
    b3447
    See related
    ASAP:ABE-0011257
    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
    ECK3431
    Summary
    Small subunit is residues 26-390; large subunit is residues 391-580. [More information is available at EcoGene: EG10374]. The ggt gene encodes -glutamyltranspeptidase . [More information is available at EcoCyc: EG10374].
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    Genomic context

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    Sequence:
    NC_000913.3 (3585081..3586823, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene uncharacterized protein YrhD Neighboring gene putative heat shock chaperone Neighboring gene DUF2756 domain-containing protein YhhA Neighboring gene glycerophosphodiester phosphodiesterase UgpQ Neighboring gene sn-glycerol 3-phosphate ABC transporter ATP binding subunit

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Escherichia coli K-12 can utilize an exogenous gamma-glutamyl peptide as an amino acid source, for which gamma-glutamyltranspeptidase is essential. Suzuki H, et al. J Bacteriol, 1993 Sep. PMID 8104180, Free PMC Article
    2. gamma-Glutamyltranspeptidase and gamma-glutamyl peptide ligases: fluorophosphonate and phosphonodifluoromethyl ketone analogs as probes of tetrahedral transition state and gamma-glutamyl-phosphate intermediate. Hiratake J, et al. Methods Enzymol, 2002. PMID 12418234
    3. Autocatalytic processing of gamma-glutamyltranspeptidase. Suzuki H, et al. J Biol Chem, 2002 Nov 8. PMID 12207027
    4. Improvement of the bitter taste of amino acids through the transpeptidation reaction of bacterial gamma-glutamyltranspeptidase. Suzuki H, et al. J Agric Food Chem, 2002 Jan 16. PMID 11782200
    5. [gamma-glutamyltranspeptidase: a new member of Ntn-hydrolase superfamily]. Suzuki H, et al. Tanpakushitsu Kakusan Koso, 2001 Sep. PMID 11552267

    See all (42) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. beta-N-(gamma-L(+)-glutamyl)phenylhydrazine was prepared from L-glutamine and phenylhydrazine through a transpeptidation reaction of Escherichia coli gamma-glutamyltranspeptidase (although phenylhydrazine has been reported to be an inhibitor of the enzyme).
      Title: Enzymatic synthesis of β-N-(γ-L(+)-glutamyl)phenylhydrazine with Escherichia coli γ-glutamyltranspeptidase.
    2. the Ser463 residue contributes to the enzymatic and autoprocessing activities of Escherichia coli gamma-glutamyltranspeptidase
      Title: Contribution of Ser463 residue to the enzymatic and autoprocessing activities of Escherichia coli gamma-glutamyltranspeptidase.
    3. Data describe the crystal structures of Escherichia coli gamma-glutamyltranspeptidase in complex with azaserine and acivicin, and suggest a novel method for inhibition by glutamine antagonists.
      Title: Crystal structures of Escherichia coli gamma-glutamyltranspeptidase in complex with azaserine and acivicin: novel mechanistic implication for inhibition by glutamine antagonists.
    4. N-terminus verified by Edman degradation on mature peptide
      Title: DNA sequence of the Escherichia coli K-12 gamma-glutamyltranspeptidase gene, ggt.
    5. In contrast to the human GGT1, the E. coli enzyme was a nonselective enzyme that accommodated substrates without specifically recognizing the C-terminal carboxy group of the Cys-Gly moiety
      Title: Design, synthesis, and evaluation of gamma-phosphono diester analogues of glutamate as highly potent inhibitors and active site probes of gamma-glutamyl transpeptidase.
    6. crystal structure
      Title: Crystal structures of gamma-glutamyltranspeptidase from Escherichia coli, a key enzyme in glutathione metabolism, and its reaction intermediate.
    Submit: New GeneRIF Correction

    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables acyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables gamma-glutamyl-peptidase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables glutathione hydrolase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables glutathione hydrolase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables leukotriene C4 gamma-glutamyl transferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables peptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    acts_upstream_of_or_within amino acid salvage IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in glutathione biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in glutathione catabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in glutathione metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in proteolysis IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within self proteolysis IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in outer membrane-bounded periplasmic space IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in periplasmic space IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in periplasmic space IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    glutathione hydrolase proenzyme
    NP_417904.1

    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

    1. NC_000913.3 Reference assembly

      Range
      3585081..3586823 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_417904.1 glutathione hydrolase proenzyme [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_417904.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A8S7TID5
      Conserved Domains (1) summary
      PRK09615
      Location:1 → 580
      ggt; gamma-glutamyltranspeptidase; Reviewed
    Nucleotide Protein
    Heading Accession and Version

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