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Gene_locus Report for: human-ESD

Homo sapiens (Human) esterase D (EC 3.1.1.1) formylglutathione hydrolase

Comment
Q9BVJ2 (Homo sapiens (Human) similar to esterase 10) one aa different from P10768 Human esterase D (hEstD),1 also called S-formylglutathione hydrolase (SFGH, EC 3.1.2.12), is a ubiquitous intracellular carboxylesterase (CE). hEstD can be found in blood cells and most human tissues and is one of the major CE activities detectable in cytosolic fractions of human liver. SFGH hydrolyzes a range of uncharged ester substrates in vitro, including p-nitrophenyl acetate (pNPA) and 4-methylumbelliferyl acetate. EstD is a thioesterase involved in the removal of genotoxic formaldehyde via a glutathione-dependent reaction. The enzyme may also play a role in xenobiotic metabolism. EstD can be induced in human cells by exposure to methylmethane sulfonate or phenobarbital


Relationship
Family|A85-EsteraseD-FGH
Block| X
Position in NCBI Life Tree|Homo sapiens
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)
> cellular organisms: N E > Eukaryota: N E > Opisthokonta: N E > Metazoa: N E > Eumetazoa: N E > Bilateria: N E > Deuterostomia: N E > Chordata: N E > Craniata: N E > Vertebrata: N E > Gnathostomata: N E > Teleostomi: N E > Euteleostomi: N E > Sarcopterygii: N E > Dipnotetrapodomorpha: N E > Tetrapoda: N E > Amniota: N E > Mammalia: N E > Theria: N E > Eutheria: N E > Boreoeutheria: N E > Euarchontoglires: N E > Primates: N E > Haplorrhini: N E > Simiiformes: N E > Catarrhini: N E > Hominoidea: N E > Hominidae: N E > Homininae: N E > Homo: N E > Homo sapiens: N E


Molecular evidence
Database
No mutation
1 structure:
3FCX: Crystal structure of human esterase D
No kinetic





2 substrates: 4-methylumbelliferyl-acetate, S-Formylglutathione
No inhibitor
>3 Genbank links 3 more: AL136958, M13450, AF112219
1 UniProt : P10768
1 Structure : 3FCX
2 UniProt : P10768, H7BZT7
2 Interpro : P10768, H7BZT7
2 Prodom : P10768, H7BZT7
2 Pfam : P10768, H7BZT7
2 PIRSF : P10768, H7BZT7
2 SUPERFAM : P10768, H7BZT7
1 EntrezGene : 2098
1 SNP : 2098
1 UniGene : 432491
1 HUGO HGNC : 3465
1 OMIM : 133280
1 Ensembl : ENSG00000139684
Sequence
Graphical view for this peptide sequence: human-ESD
Colored MSA for A85-EsteraseD-FGH (raw)
MALKQISSNKCFGGLQKVFEHDSVELNCKMKFAVYLPPKAETGKCPALYW
LSGLTCTEQNFISKSGYHQSASEHGLVVIAPDTSPRGCNIKGEDESWDFG
TGAGFYVDATEDPWKTNYRMYSYVTEELPQLINANFPVDPQRMSIFGHSM
GGHGALICALKNPGKYKSVSAFAPICNPVLCPWGKKAFSGYLGTDQSKWK
AYDATHLVKSYPGSQLDILIDQGKDDQFLLDGQLLPDNFIAACTEKKIPV
VFRLQEGYDHSYYFIATFITDHIRHHAKYLNA
Legend This sequence has been compared to family alignement (MSA)
red => minority aminoacid
blue => majority aminoacid
color intensity => conservation rate
title => sequence position(MSA position)aminoacid rate
Catalytic site
Catalytic site in the MSA

MALKQISSNKCFGGLQKVFEHDSVELNCKMKFAVYLPPKAETGKCPALYW
LSGLTCTEQNFISKSGYHQSASEHGLVVIAPDTSPRGCNIKGEDESWDFG
TGAGFYVDATEDPWKTNYRMYSYVTEELPQLINANFPVDPQRMSIFGHSM
GGHGALICALKNPGKYKSVSAFAPICNPVLCPWGKKAFSGYLGTDQSKWK
AYDATHLVKSYPGSQLDILIDQGKDDQFLLDGQLLPDNFIAACTEKKIPV
VFRLQEGYDHSYYFIATFITDHIRHHAKYLNA


References
5 more
    Title: Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning
    Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB and Chen JL <19 more author(s)>
    Ref: Proc Natl Acad Sci U S A, 97:9543, 2000 : PubMed

            

    Title: Human esterase D gene: complete cDNA sequence, genomic structure, and application in the genetic diagnosis of human retinoblastoma
    Young LJ, Lee EY, To HA, Bookstein R, Shew JY, Donoso LA, Sery T, Giblin M, Shields JA, Lee WH
    Ref: Hum Genet, 79:137, 1988 : PubMed

            

    Title: Molecular cloning of the human esterase D gene, a genetic marker of retinoblastoma
    Lee EY, Lee WH
    Ref: Proc Natl Acad Sci U S A, 83:6337, 1986 : PubMed

            


Other Papers


Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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