UniProt functional annotation for Q52VH2



	UniProt functional annotation for Q52VH2

UniProt code: Q52VH2.

Organism: Sphingosinicella xenopeptidilytica.

Taxonomy: Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; Sphingomonadaceae; Sphingosinicella.

Function: Beta-aminopeptidase that can cleave synthetic beta-peptides which consist of backbone-elongated beta-amino acid residues that are not processed by common proteolytic enzymes. Can cleave the beta- peptides beta-homoVal-beta-homoAla-beta-homoLeu and beta-homoAla-beta- homoLeu. Requires a beta-amino acid at the N-terminus of peptide substrates and cleaves the peptide bond between the N-terminal beta- amino acid and the amino acid at the second position of tripeptidic substrates of the general structure H-betahXaa-Ile-betahTyr-OH according to the following preferences with regard to the side chain of the N-terminal beta-amino acid: aliphatic and aromatic > OH-containing > hydrogen, basic and polar. {ECO:0000269|PubMed:16109932, ECO:0000269|PubMed:17064315}.

Catalytic activity: Reaction=Cleaves N-terminal beta-homoamino acids from peptides composed of 2 to 6 amino acids.; EC=3.4.11.25; Evidence={ECO:0000269|PubMed:16109932, ECO:0000269|PubMed:17064315, ECO:0000269|PubMed:22961926, ECO:0000269|PubMed:22980995};

Activity regulation: Inhibited by AEBSF (4-(2- aminoethyl)benzenesulfonyl fluoride, Pefabloc SC), ampicillin and AMP(hyd) (ampillicin-derived penicilloic acid). {ECO:0000269|PubMed:17064315, ECO:0000269|PubMed:22961926, ECO:0000269|PubMed:22980995}.

Biophysicochemical properties: Kinetic parameters: KM=9.0 mM for beta-homoVal-beta-homoAla-beta-homoLeu {ECO:0000269|PubMed:17064315}; KM=20 mM for beta-homoAla-beta-homoLeu {ECO:0000269|PubMed:17064315}; KM=8.2 mM for beta-homoGly-pNA {ECO:0000269|PubMed:17064315}; KM=1.2 mM for beta-homoAla-pNA {ECO:0000269|PubMed:22961926}; Vmax=3.1 umol/min/mg enzyme with beta-homoVal-beta-homoAla-beta- homoLeu as substrate {ECO:0000269|PubMed:17064315}; Vmax=1.1 umol/min/mg enzyme with beta-homoAla-beta-homoLeu as substrate {ECO:0000269|PubMed:17064315}; Vmax=0.026 umol/min/mg enzyme with carnosine as substrate {ECO:0000269|PubMed:17064315}; Vmax=0.98 umol/min/mg enzyme with beta-homoVal-Ile-beta-homoTyr as substrate {ECO:0000269|PubMed:17064315}; Vmax=1.9 umol/min/mg enzyme with beta-homoVal-Ile-beta-homoTyr as substrate {ECO:0000269|PubMed:17064315}; Vmax=0.68 umol/min/mg enzyme with beta-homoPhe-Ile-beta-homoTyr as substrate {ECO:0000269|PubMed:17064315}; Vmax=0.47 umol/min/mg enzyme with beta-homoTyr-Ile-beta-homoTyr as substrate {ECO:0000269|PubMed:17064315}; Vmax=0.047 umol/min/mg enzyme with beta-homoTrp-Ile-beta-homoTyr as substrate {ECO:0000269|PubMed:17064315}; Vmax=0.095 umol/min/mg enzyme with beta-homoSer-Ile-beta-homoTyr as substrate {ECO:0000269|PubMed:17064315}; Vmax=0.068 umol/min/mg enzyme with beta-homoThr-Ile-beta-homoTyr as substrate {ECO:0000269|PubMed:17064315}; Vmax=0.017 umol/min/mg enzyme with beta-homoLys-Ile-beta-homoTyr as substrate {ECO:0000269|PubMed:17064315}; Vmax=0.028 umol/min/mg enzyme with D-beta-homoVal-Ile-beta-homoTyr as substrate {ECO:0000269|PubMed:17064315}; Vmax=16.4 umol/min/mg enzyme with beta-homoAla-pNA as substrate {ECO:0000269|PubMed:22961926}; pH dependence: Optimum pH is between 8 and 9. {ECO:0000269|PubMed:17064315};

Subunit: Heterooctamer of 4 heterodimers ((alpha:beta)4); each heterodimer is composed of an alpha subunit and a beta subunit processed from the same precursor. {ECO:0000269|PubMed:16109932, ECO:0000269|PubMed:22961926, ECO:0000269|PubMed:22980995}.

Subcellular location: Periplasm {ECO:0000303|PubMed:16109932}.

Ptm: Autoproteolytic processing to generate the alpha and beta subunit is required for self-activation and is proposed to use a similar mechanism as substrate cleavage. {ECO:0000303|PubMed:22980995}.

Similarity: Belongs to the peptidase S58 family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Sphingosinicella xenopeptidilytica.
Taxonomy:		Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; Sphingomonadaceae; Sphingosinicella.



Function:		Beta-aminopeptidase that can cleave synthetic beta-peptides which consist of backbone-elongated beta-amino acid residues that are not processed by common proteolytic enzymes. Can cleave the beta- peptides beta-homoVal-beta-homoAla-beta-homoLeu and beta-homoAla-beta- homoLeu. Requires a beta-amino acid at the N-terminus of peptide substrates and cleaves the peptide bond between the N-terminal beta- amino acid and the amino acid at the second position of tripeptidic substrates of the general structure H-betahXaa-Ile-betahTyr-OH according to the following preferences with regard to the side chain of the N-terminal beta-amino acid: aliphatic and aromatic > OH-containing > hydrogen, basic and polar. {ECO:0000269\|PubMed:16109932, ECO:0000269\|PubMed:17064315}.


Catalytic activity:		Reaction=Cleaves N-terminal beta-homoamino acids from peptides composed of 2 to 6 amino acids.; EC=3.4.11.25; Evidence={ECO:0000269\|PubMed:16109932, ECO:0000269\|PubMed:17064315, ECO:0000269\|PubMed:22961926, ECO:0000269\|PubMed:22980995};
Activity regulation:		Inhibited by AEBSF (4-(2- aminoethyl)benzenesulfonyl fluoride, Pefabloc SC), ampicillin and AMP(hyd) (ampillicin-derived penicilloic acid). {ECO:0000269\|PubMed:17064315, ECO:0000269\|PubMed:22961926, ECO:0000269\|PubMed:22980995}.
Biophysicochemical properties:		Kinetic parameters: KM=9.0 mM for beta-homoVal-beta-homoAla-beta-homoLeu {ECO:0000269\|PubMed:17064315}; KM=20 mM for beta-homoAla-beta-homoLeu {ECO:0000269\|PubMed:17064315}; KM=8.2 mM for beta-homoGly-pNA {ECO:0000269\|PubMed:17064315}; KM=1.2 mM for beta-homoAla-pNA {ECO:0000269\|PubMed:22961926}; Vmax=3.1 umol/min/mg enzyme with beta-homoVal-beta-homoAla-beta- homoLeu as substrate {ECO:0000269\|PubMed:17064315}; Vmax=1.1 umol/min/mg enzyme with beta-homoAla-beta-homoLeu as substrate {ECO:0000269\|PubMed:17064315}; Vmax=0.026 umol/min/mg enzyme with carnosine as substrate {ECO:0000269\|PubMed:17064315}; Vmax=0.98 umol/min/mg enzyme with beta-homoVal-Ile-beta-homoTyr as substrate {ECO:0000269\|PubMed:17064315}; Vmax=1.9 umol/min/mg enzyme with beta-homoVal-Ile-beta-homoTyr as substrate {ECO:0000269\|PubMed:17064315}; Vmax=0.68 umol/min/mg enzyme with beta-homoPhe-Ile-beta-homoTyr as substrate {ECO:0000269\|PubMed:17064315}; Vmax=0.47 umol/min/mg enzyme with beta-homoTyr-Ile-beta-homoTyr as substrate {ECO:0000269\|PubMed:17064315}; Vmax=0.047 umol/min/mg enzyme with beta-homoTrp-Ile-beta-homoTyr as substrate {ECO:0000269\|PubMed:17064315}; Vmax=0.095 umol/min/mg enzyme with beta-homoSer-Ile-beta-homoTyr as substrate {ECO:0000269\|PubMed:17064315}; Vmax=0.068 umol/min/mg enzyme with beta-homoThr-Ile-beta-homoTyr as substrate {ECO:0000269\|PubMed:17064315}; Vmax=0.017 umol/min/mg enzyme with beta-homoLys-Ile-beta-homoTyr as substrate {ECO:0000269\|PubMed:17064315}; Vmax=0.028 umol/min/mg enzyme with D-beta-homoVal-Ile-beta-homoTyr as substrate {ECO:0000269\|PubMed:17064315}; Vmax=16.4 umol/min/mg enzyme with beta-homoAla-pNA as substrate {ECO:0000269\|PubMed:22961926}; pH dependence: Optimum pH is between 8 and 9. {ECO:0000269\|PubMed:17064315};
Subunit:		Heterooctamer of 4 heterodimers ((alpha:beta)4); each heterodimer is composed of an alpha subunit and a beta subunit processed from the same precursor. {ECO:0000269\|PubMed:16109932, ECO:0000269\|PubMed:22961926, ECO:0000269\|PubMed:22980995}.
Subcellular location:		Periplasm {ECO:0000303\|PubMed:16109932}.
Ptm:		Autoproteolytic processing to generate the alpha and beta subunit is required for self-activation and is proposed to use a similar mechanism as substrate cleavage. {ECO:0000303\|PubMed:22980995}.
Similarity:		Belongs to the peptidase S58 family. {ECO:0000305}.