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Renal dipeptidase (rDP) (EC 3.4.13.19), also known as microsomal dipeptidase or membrane dipeptidase, is a zinc-dependent metalloenzyme which hydrolyzes a wide range of dipeptides. It is involved in renal metabolism of glutathione and its conjugates. It is a homodimeric disulfide-linked glycoprotein attached to the renal brush border microvilli membrane by a GPI-anchor.

The active site of rDP is composed of binuclear zinc ions bridged by a glutamate residue [1,2]. The two zinc ions are coordinated by three different histidine residues, the glutamate and an aspartate (see <PDB:1ITU>). Four cysteine residues form two disulfide bonds and an additional cysteine residue in the C-terminal part links to the corresponding cysteine of the other subunit in the homodimeric enzyme.

RDP seems to be evolutionary related to hypothetical proteins in the PQQ biosynthesis operons of Acinetobacter calcoaceticus and Klebsiella pneumoniae. We selected for a signature pattern the region around the glutamate residue in the active site, which is highly conserved. We also developed a profile that covers the entire renal dipeptidase.

February 2008 / Text revised; profile added.

These proteins belong to family M19 in the classification of peptidases [3,E1].

PROSITE methods (with tools and information) covered by this documentation:

RENAL_DIPEPTIDASE_2, PS51365; Renal dipeptidase family profile  (MATRIX)

Sequences known to belong to this class detected by the profile: ALL Other sequence(s) detected in Swiss-Prot: NONE.

• Domain architecture view of Swiss-Prot proteins matching PS51365 • Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS51365 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS51365 • Scan Swiss-Prot/TrEMBL entries against PS51365 • view ligand binding statistics

Matching PDB structures: 1ITQ 1ITU [ALL]

RENAL_DIPEPTIDASE_1, PS00869; Renal dipeptidase active site  (PATTERN)

Consensus pattern: [LIVM]-E-G-[GA]-x(2)-[LIVMF]-x(6)-L-x(3)-Y-x(2)-G-[LIVM]-R E is a zinc ligand Sequences known to belong to this class detected by the pattern: ALL Other sequence(s) detected in Swiss-Prot: NONE.

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00869 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00869 • Scan Swiss-Prot/TrEMBL entries against PS00869 • view ligand binding statistics

Matching PDB structures: 1ITQ 1ITU [ALL]

1	Authors	Adachi H., Katayama T., Nakazato H., Tsujimoto M.
	Title	Importance of Glu-125 in the catalytic activity of human renal dipeptidase.
	Source	Biochim. Biophys. Acta 1163:42-48(1993).
	PubMed ID	8097406

2	Authors	Nitanai Y., Satow Y., Adachi H., Tsujimoto M.
	Title	Crystal structure of human renal dipeptidase involved in beta-lactam hydrolysis.
	Source	J. Mol. Biol. 321:177-184(2002).
	PubMed ID	12144777

3	Authors	Rawlings N.D., Barrett A.J.
	Title	Evolutionary families of metallopeptidases.
	Source	Methods Enzymol. 248:183-228(1995).
	PubMed ID	7674922

E1
Source	http://www.uniprot.org/docs/peptidas

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