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Overview for MACiE Entry M0168

Version history

General Information

EC Number: 3.4.13.19 (A member of the Hydrolases, Acting on peptide bonds (peptidases), Dipeptidases)

Enzyme Name: membrane dipeptidase

Biological Species: Homo sapiens (Human)

Catalytic Chain UniprotKB Accession Codes:

Representative PDB Code: 1itq - HUMAN RENAL DIPEPTIDASE (Resolution = 2.30 Å).

Catalytic CATH Codes:

Display structure information

Overall Reaction:

Image of dipeptide

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dipeptide
C00107
CHEBI:46761
water
C00001
CHEBI:15377
2 amino acid
C00045
CHEBI:59869

Overall Comment: Hydrolises dipeptides in general.


View similar reactions


Stepwise Description of the Reaction

Step 1Asp288 deprotonates the zinc activated water molecule.
Step 2The activated hydroxide attacks the peptide carbonyl in a nucleophilic addition.
Step 3The oxyanion initiates an elimination that cleaves the peptide bond, releasing the amino acid products, the N-terminus then protonates from Asp288

View similar reactions (composite manual annotation)


Catalytic Residues Involved

Type Number Chain Location of Function
His 152 A Side Chain
Asp 288 A Side Chain

Metal Cofactors for M0168

Type Het group Number Chain
zinc ZN 401 A Overview
zinc ZN 402 A Overview

References

  1. Y. Nitanai et al. (2002), J. Mol. Biol., 321, 177-184. Crystal structure of human renal dipeptidase involved in beta-lactam hydrolysis.
    Medline: 12144777

Homologue information for M0168 (1itq)

CSA Homologues

MACiE Homologues (within the PDB)

MACiE Homologues (within UniprotKB/SwissProt)



Entries with at least one Catalytic CATH code in common (different mechanisms):

MACiE Entry Enzyme Name
EC Number
PDB code CATH code Composite
Reaction Similarity
Catalytic Machinery
Similarity
M0159 aryldialkylphosphatase
3.1.8.1
1hzy 3.20.20.140
0.19480.6956Compare
M0172 isoaspartyl dipeptidase
3.4.19.-
1onw 3.20.20.140
0.55550.45Compare
M0087 urease
3.5.1.5
1fwj 3.20.20.140
0.4090.5388Compare

View a comparison of the other reactions in MACiE with the CATH domain 3.20.20.140


Links to this entry in other databases

Link to EC-PDB-SUM Link to PDB-SUM Link to RCSB PDB Link to PDBe Link to CSA
Link to MetaCyc Link to KEGG Link to BRENDA Link to ExplorENZ
Link to SFLD

GOA logo
protein binding (molecular function)
plasma membrane (cellular component)
proteolysis (biological process)
peptidase activity (molecular function)
metalloexopeptidase activity (molecular function)
dipeptidyl-peptidase activity (molecular function)
apical plasma membrane (cellular component)
dipeptidase activity (molecular function)
anchored component of membrane (cellular component)
microvillus membrane (cellular component)
cell projection (cellular component)
metal ion binding (molecular function)
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