P0CX77 · ASP22_YEAST

Function

Miscellaneous

Yeast contains 2 L-asparaginase isoenzymes: cytoplasmic L-asparaginase I, and cell wall L-asparaginase II.
There are 4 copies for L-asparaginase 2 in yeast. The 4 identical copies ASP3-1, ASP3-2, ASP3-3 and ASP3-4 are arranged in tandem repeats located near a ribosomal DNA cluster.

Catalytic activity

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
0.27 mML-asparagine
0.27 mMD-asparagine
0.27 mMN-acetyl-L-asparagine
0.07 mMN-carbamyl-L-asparagine
0.06 mMN-isoleucyl-L-asparagine
0.06 mMN-glycyl-L-asparagine
0.06 mMN-valyl-L-asparagine
0.2 mMN-methionyl-L-asparagine
0.4 mMN-glycyl-D-asparagine
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
42 μmol/min/mgfor L-asparagine
60 μmol/min/mgfor D-asparagine
167 μmol/min/mgfor N-acetyl-L-asparagine
79 μmol/min/mgfor N-carbamyl-L-asparagine
67 μmol/min/mgfor N-isoleucyl-L-asparagine
135 μmol/min/mgfor N-glycyl-L-asparagine
56 μmol/min/mgfor N-valyl-L-asparagine
92 μmol/min/mgfor N-methionyl-L-asparagine
8 μmol/min/mgfor N-glycyl-D-asparagine
Does not act on isoasparagine, L-aspartate diamide, beta-alanine amide and L-glutamine.

pH Dependence

Optimum pH is 6.8. Active from pH 5.5 to pH 7.5. Stable from pH 3.5 to pH 10.5.

Features

Showing features for active site, binding site.

Type
IDPosition(s)Description
Active site43O-isoaspartyl threonine intermediate
Binding site89substrate
Binding site122-123substrate

GO annotations

AspectTerm
Cellular Componentcell wall-bounded periplasmic space
Cellular Componentextracellular region
Cellular Componentperiplasmic space
Molecular Functionasparaginase activity
Biological Processasparagine catabolic process
Biological Processcellular response to nitrogen starvation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    L-asparaginase 2-2
  • EC number
  • Alternative names
    • L-asparaginase II
    • L-asparagine amidohydrolase II (ASP II)

Gene names

    • Name
      ASP3-2
    • ORF names
      L9632.7
    • Ordered locus names
      YLR157C

Organism names

Accessions

  • Primary accession
    P0CX77
  • Secondary accessions
    • D6VYF3
    • P11163
    • Q12268
    • Q6Q5K8
    • Q6Q5K9

Proteomes

Organism-specific databases

Phenotypes & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variant26-55

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 1 variant from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for signal, chain, glycosylation.

Type
IDPosition(s)Description
Signal1-25
ChainPRO_000041044126-362L-asparaginase 2-2
Glycosylation29N-linked (GlcNAc...) asparagine
Glycosylation93N-linked (GlcNAc...) asparagine
Glycosylation239N-linked (GlcNAc...) asparagine

Keywords

Proteomic databases

PTM databases

Expression

Induction

Subject to nitrogen catabolite repression (NCR). Not found in cells grown on rich nitrogen sources like ammonia, glutamine or glutamate, but is found in cells that have been subjected to nitrogen starvation or have been grown on a poor nitrogen source such as proline.

Gene expression databases

Interaction

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain33-359Asparaginase/glutaminase

Sequence similarities

Belongs to the asparaginase 1 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    362
  • Mass (Da)
    38,687
  • Last updated
    2011-06-28 v1
  • Checksum
    1DE5DC8692BF0461
MRSLNTLLLSLFVAMSSGAPLLKIREEKNSSLPSIKIFGTGGTIASKGSTSATTAGYSVGLTVNDLIEAVPSLAEKANLDYLQVSNVGSNSLNYTHLIPLYHGISEALASDDYAGAVVTHGTDTMEETAFFLDLTINSEKPVCIAGAMRPATATSADGPMNLYQAVSIAASEKSLGRGTMITLNDRIASGFWTTKMNANSLDTFRADEQGYLGYFSNDDVEFYYPPVKPNGWQFFDISNLTDPSEIPEVIILYSYQGLNPELIVKAVKDLGAKGIVLAGSGAGSWTATGSIVNEQLYEEYGIPIVHSRRTADGTVPPDDAPEYAIGSGYLNPQKSRILLQLCLYSGYGMDQIRSVFSGVYGG

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict243in Ref. 4; AAS56284

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U51921
EMBL· GenBank· DDBJ
AAB67481.1
EMBL· GenBank· DDBJ
Genomic DNA
AY557958
EMBL· GenBank· DDBJ
AAS56284.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006945
EMBL· GenBank· DDBJ
DAA09472.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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