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MGP005967

UniProt Annotations

Entry Information
Gene Nameasparaginase like 1
Protein EntryASGL1_HUMAN
UniProt IDQ7L266
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q7L266-1; Sequence=Displayed; Name=2; IsoId=Q7L266-2; Sequence=VSP_028287; Note=No experimental confirmation available.;
Biophysicochemical PropertiesKinetic parameters: KM=3.4 mM for L-asparagine (L-Asn) {ECO:0000269|PubMed:19839645}; KM=0.4 mM for L-aspartic acid beta-methyl ester {ECO:0000269|PubMed:19839645}; KM=0.4 mM for L-Asp-L-Phe {ECO:0000269|PubMed:19839645}; KM=1.0 mM for L-Asp-L-Ala {ECO:0000269|PubMed:19839645};
Catalytic ActivityCleavage of a beta-linked Asp residue from the N-terminus of a polypeptide.
Catalytic ActivityL-asparagine + H(2)O = L-aspartate + NH(3).
Enzyme RegulationGlycine accelerates autocleavage into an alpha and beta chain. {ECO:0000269|PubMed:22861376}.
FunctionHas both L-asparaginase and beta-aspartyl peptidase activity. May be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions. Is highly active with L-Asp beta-methyl ester. Besides, has catalytic activity toward beta-aspartyl dipeptides and their methyl esters, including beta-L-Asp-L-Phe, beta-L-Asp-L-Phe methyl ester (aspartame), beta-L-Asp-L-Ala, beta-L-Asp-L-Leu and beta-L- Asp-L-Lys. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine. {ECO:0000269|PubMed:19839645}.
InductionBy 5-alpha-di-hydrotestosterone and progesterone. {ECO:0000269|PubMed:14654938}.
PtmCleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity.
Sequence CautionSequence=BAB15302.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; Sequence=BAB15302.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
SimilarityBelongs to the Ntn-hydrolase family. {ECO:0000305}.
Subcellular LocationCytoplasm {ECO:0000269|PubMed:11984834}. Note=Midpiece of sperm tail.
SubunitHeterodimer of an alpha and beta chain produced by autocleavage. This heterodimer may then dimerize in turn, giving rise to a heterotetramer. {ECO:0000269|PubMed:22861376, ECO:0000269|PubMed:22891768}.
Tissue SpecificityExpressed in brain, kidney, testis and tissues of the gastrointestinal tract. Present in sperm (at protein level). Over-expressed in uterine, mammary, prostatic and ovarian carcinoma. {ECO:0000269|PubMed:11984834, ECO:0000269|PubMed:14654938}.
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