B3EWR5 · HEXL_LUPAL
- ProteinBeta-hexosaminidase
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Has hexosaminidase activity. Active with both p-nitrophenyl-beta-D-N-acetylglucosamine (pNP-GlcNAc) and p-nitrophenyl-beta-D-N-acetylgalactosamine (pNP-GalNAc). Not active toward p-nitrophenyl-beta-D-N,N'-diacetylchitobiose (pNP-(GlcNAc)2) or p-nitrophenyl-beta-D-N,N',N''-triacetylchitobiose (pNP-(GlcNAc)3). Removes terminal GlcNAc and may be involved in storage protein degradation.
Catalytic activity
Activity regulation
Inhibited by AgNO3 at a concentration of 0.1 mM. Strongly inhibited by CdCl2, ZnCl2 and FeCl3 and moderately by CoCl2, CuSO4 and NiCl2 at 10 mM concentration. CaCl2, MgCl2, MnSO4 and KI also have a slight inhibitory effect of 20%-25% at 10 mM concentration. Activated to a small extent by MgCl2 at 0.1 mM concentration but inhibited with increasing concentration. Not affected by carbohydrates such as fucose, galactose and glucose but displays a slight decrease in activity up to 25% with lactose, alpha-mannose and N-acetyl-galactosamine (GalNAc).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
2.59 mM | pNP-GlcNAc | |||||
2.94 mM | pNP-GalcNAc |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
18.4 μmol/min/mg | with pNP-GlcNAc as substrate | ||||
2.73 μmol/min/mg | with pNP-GalcNAc as substrate |
pH Dependence
Optimum pH is 5.0 with pNP-GlcNAc and 4.0 with pNP-GalNAc. Half maximal activity observed at pH 3.0 and 6.5 with pNP-GlcNAc and at pH 2.5 and 5.5 with pNP-GalNAc. Retains over 90% of its activity between pH 6.5-8.0 with pNP-GlcNAc, and between pH 6.0-7.5 with pNP-GalNAc.
Temperature Dependence
Optimum temperature is 50 degrees Celsius toward pNP-GlcNAc and 60 degrees Celsius toward pNP-GalNAc. Displays activity higher than 50% between 35-70 degrees Celsius. Stable under 30 degrees Celsius.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | beta-N-acetylhexosaminidase activity | |
Molecular Function | N-acetyl-beta-D-galactosaminidase activity |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBeta-hexosaminidase
- EC number
- Alternative names
Organism names
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fabales > Fabaceae > Papilionoideae > 50 kb inversion clade > genistoids sensu lato > core genistoids > Genisteae > Lupinus
Accessions
- Primary accessionB3EWR5
PTM/Processing
Features
Showing features for peptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Peptide | PRO_0000422556 | 1-26 | Beta-hexosaminidase | |||
Sequence: VDSEDLIEAFKIYVEDDNEHLQGSVD |
Post-translational modification
Glycosylated.
Keywords
- PTM
Expression
Tissue specificity
Detected in dry seeds and cotyledons.
Developmental stage
Activity levels increase 5-9 days after imbibition in the hypocotyls and within 3-9 days in the roots. Detected in dry seeds but increased levels observed 5 days after seed imbibition.
Structure
Family & Domains
Family and domain databases
Sequence
- Sequence statusFragment
- Length26
- Mass (Da)2,980
- Last updated2013-11-13 v2
- Checksum5F04E3EC26FC875D
Features
Showing features for sequence uncertainty, non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence uncertainty | 8 | E or N | ||||
Sequence: E | ||||||
Non-terminal residue | 26 | |||||
Sequence: D |
Keywords
- Technical term