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Index > Protein center > CCBL1(Gene name) > Human
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  • CCBL1 (Gene name),
  • Kynurenine--oxoglutarate transaminase 1 (Protein name ),  KAT1_HUMAN from NCBI database.
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  • General Annotation
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  • Antigen Annotation
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  • Gene name:
    CCBL1;
    Protein name:
    Kynurenine--oxoglutarate transaminase 1;
    Alternative:
    Glutamine transaminase K(GTK);4.4.1.13;Cysteine-S-conjugate beta-lyase);Kynurenine aminotransferase I(KATI);2.6.1.64;Glutamine--phenylpyruvate transaminase);Kynurenine--oxoglutarate transaminase I;
    Organism:
    Human (Homo sapiens). 
    General Annotation
    Sub Unit:
    Homodimer.
    Function:
    Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Catalyzes the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond.
    Subcellular Location:
    Cytoplasm
    Protein Attributes:
    Sequence length:
    422
    Sequence:
    50:
    MAKQLQARRL | DGIDYNPWVE | FVKLASEHDV | VNLGQGFPDF | PPPDFAVEAF | 
    100:
    QHAVSGDFML | NQYTKTFGYP | PLTKILASFF | GELLGQEIDP | LRNVLVTVGG | 
    150:
    YGALFTAFQA | LVDEGDEVII | IEPFFDCYEP | MTMMAGGRPV | FVSLKPGPIQ | 
    200:
    NGELGSSSNW | QLDPMELAGK | FTSRTKALVL | NTPNNPLGKV | FSREELELVA | 
    250:
    SLCQQHDVVC | ITDEVYQWMV | YDGHQHISIA | SLPGMWERTL | TIGSAGKTFS | 
    300:
    ATGWKVGWVL | GPDHIMKHLR | TVHQNSVFHC | PTQSQAAVAE | SFEREQLLFR | 
    350:
    QPSSYFVQFP | QAMQRCRDHM | IRSLQSVGLK | PIIPQGSYFL | ITDISDFKRK | 
    400:
    MPDLPGAVDE | PYDRRFVKWM | IKNKGLVAIP | VSIFYSVPHQ | KHFDHYIRFC | 
    422:
    FVKDEATLQA | MDEKLRKWKV | EL
    3D Structure:
    N/A
    Predicted Eptitope:
    Please Sign in.
    EIAab Sequence  Vaild Sequence:
    Please Sign in.
    Related Databases
    KEGG:
    UniGene:
    MIM:
    Pfam:
    String:
    SMR:
    Uniprot:
     
    FOR
    ELISA Kit for Human Kynurenine--oxoglutarate transaminase 1
    Cat.:
    E0282h
    Price:
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    MSDS:
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    Packing:
    96T
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    ELISA Kit for Human Kynurenine--oxoglutarate transaminase 1
    Cat.:
    E0282r
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    MSDS:
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    Packing:
    96T
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    ELISA Kit for Human Kynurenine--oxoglutarate transaminase 1
    Cat.:
    E0282m
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    MSDS:
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    Packing:
    96T
    CLIA Kit for Human Kynurenine--oxoglutarate transaminase 1
    Cat.:
    U0282r
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    MSDS:
    Please sign in first.
    Packing:
    96T
    CLIA Kit for Human Kynurenine--oxoglutarate transaminase 1
    Cat.:
    U0282h
    Price:
    Please sign in first.
    MSDS:
    Please sign in first.
    Packing:
    96T
    Range:
    Please sign in first.
    CLIA Kit for Human Kynurenine--oxoglutarate transaminase 1
    Cat.:
    U0282m
    Price:
    Please sign in first.
    MSDS:
    Please sign in first.
    Packing:
    96T
    Polyclonal Antibody for Human Kynurenine--oxoglutarate transaminase 1
    Cat.:
    P0282Rb-h
    Price:
    Please sign in first.
    Packing:
    40ug/0.2ml
    Polyclonal Antibody for Human Kynurenine--oxoglutarate transaminase 1
    Cat.:
    P0282Rb-m
    Price:
    Please sign in first.
    Packing:
    40ug/0.2ml
    Polyclonal Antibody for Human Kynurenine--oxoglutarate transaminase 1
    Cat.:
    P0282Rb-r
    Price:
    Please sign in first.
    Packing:
    40ug/0.2ml
    Monoclonal Antibody for Human Kynurenine--oxoglutarate transaminase 1
    Monoclonal Antibody for Human Kynurenine--oxoglutarate transaminase 1
    Monoclonal Antibody for Human Kynurenine--oxoglutarate transaminase 1
    Protein for Human Kynurenine--oxoglutarate transaminase 1
    Protein for Human Kynurenine--oxoglutarate transaminase 1
    Protein for Human Kynurenine--oxoglutarate transaminase 1

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    Precision
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    Recovery
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    Linearity
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    References
    1. 1.
      "Molecular cloning and expression of a cDNA for human kidney cysteine conjugate beta-lyase."
      Perry S. , Harries H. , Scholfield C. , Lock E. , King L. , Gibson G. , Goldfarb P.
      FEBS Lett.360:277-280(1995) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)
      tissue: Kidney.
    2. 2.
      "DNA sequence and analysis of human chromosome 9."
      Humphray S.J. , Oliver K. , Hunt A.R. , Plumb R.W. , Loveland J.E. , Howe K.L. , Andrews T.D. , Searle S. , Hunt S.E. , Scott C.E. , Jones M.C. , Ainscough R. , Almeida J.P. , Ambrose K.D. , Ashwell R.I.S. , Babbage A.K. , Babbage S. , Bagguley C.L. , more...
      Nature429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]
    3. 3.
      "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res.14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3)
      tissue: Brain.
      tissue: Muscle.
    4. 4.
      "Crystal structure of human kynurenine aminotransferase I."
      Rossi F. , Han Q. , Li J. , Li J. , Rizzi M.
      J. Biol. Chem.279:50214-50220(2004) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE AND PHENYLALANINE;SUBUNIT;COFACTOR
    5. 5.
      "Structural insight into the inhibition of human kynurenine aminotransferase I/glutamine transaminase K."
      Han Q. , Robinson H. , Cai T. , Tagle D.A. , Li J.
      J. Med. Chem.52:2786-2793(2009) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEXES WITH PYRIDOXAL PHOSPHATE AND THE INHIBITORS INDOLEACETIC ACID AND TRIS;FUNCTION;CATALYTIC ACTIVITY;ENZYME REGULATION;COFACTOR
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