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Protein

Beta-hexosaminidase

Gene
N/A
Organism
Lupinus albus (White lupin) (Lupinus termis)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.1 Publication

Enzyme regulationi

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).1 Publication

Kineticsi

  1. KM=2.59 mM for pNP-GlcNAc1 Publication
  2. KM=2.94 mM for pNP-GalcNAc1 Publication
  1. Vmax=18.4 µmol/min/mg enzyme with pNP-GlcNAc as substrate1 Publication
  2. Vmax=2.73 µmol/min/mg enzyme with pNP-GalcNAc as substrate1 Publication

pH dependencei

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.1 Publication

Temperature dependencei

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.1 Publication

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-hexosaminidase (EC:3.2.1.52)
Alternative name(s):
Beta-GlcNAcase
Beta-N-acetylhexosaminidase
Short name:
Beta-NAHase
N-acetyl-beta-glucosaminidase
OrganismiLupinus albus (White lupin) (Lupinus termis)
Taxonomic identifieri3870 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeGenisteaeLupinus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Peptidei1 – ›26›26Beta-hexosaminidasePRO_0000422556Add
BLAST

Post-translational modificationi

Glycosylated.1 Publication

Keywords - PTMi

Glycoprotein

Expressioni

Tissue specificityi

Detected in dry seeds and cotyledons.1 Publication

Developmental stagei

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.1 Publication

Sequencei

Sequence statusi: Fragment.

B3EWR5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20 
VDSEDLIEAF KIYVEDDNEH LQGSVD
Length:26
Mass (Da):2,980
Last modified:November 13, 2013 - v2
Checksum:i5F04E3EC26FC875D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence uncertaintyi8 – 81E or N
Non-terminal residuei26 – 261

Cross-referencesi

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

ProtoNetiSearch...

Publicationsi

  1. "beta-N-Acetylhexosaminidase involvement in alpha-conglutin mobilization in Lupinus albus."
    Santos C.N., Alves M., Oliveira A., Ferreira R.B.
    J. Plant Physiol. 170:1047-1056(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, GLYCOSYLATION.
    Tissue: Cotyledon.

Entry informationi

Entry nameiHEXL_LUPAL
AccessioniPrimary (citable) accession number: B3EWR5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2013
Last sequence update: November 13, 2013
Last modified: October 1, 2014
This is version 6 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.