Detail Information for IndEnz0002002435
IED ID IndEnz0002002435
Enzyme Type ID protease002435
Protein Name D-alanyl-D-alanine dipeptidase
D-Ala-D-Ala dipeptidase
EC 3.4.13.22
Gene Name ddpX vanX yddT b1488 JW1483
Organism Escherichia coli (strain K12)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12)
Enzyme Sequence MSDTTELVDLAVIFPDLEIELKYACADNITGKAIYQQARCLLHKDAITALAKSISIAQLSGLQLVIYDAYRPQQAQAMLWQACPDPQYVVDVTVGSNHSRGTAIDLTLRDEHGNILDMGAGFDEMHERSHAYHPSVPPAAQRNRLLLNAIMTGGGFVGISSEWWHFELPQAASYPLLADQFSCFISPGTQHVS
Enzyme Length 193
Uniprot Accession Number P77790
Absorption
Active Site ACT_SITE 162; /note=Proton donor/acceptor; /evidence=ECO:0000255|HAMAP-Rule:MF_01924
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=D-alanyl-D-alanine + H2O = 2 D-alanine; Xref=Rhea:RHEA:20661, ChEBI:CHEBI:15377, ChEBI:CHEBI:57416, ChEBI:CHEBI:57822; EC=3.4.13.22; Evidence={ECO:0000255|HAMAP-Rule:MF_01924, ECO:0000269|PubMed:9751644};
DNA Binding
EC Number 3.4.13.22
Enzyme Function FUNCTION: Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide. May have a role in cell-wall turnover. {ECO:0000255|HAMAP-Rule:MF_01924, ECO:0000269|PubMed:9751644}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Metal binding (3); Site (1)
Keywords Cell wall biogenesis/degradation;Cytoplasm;Dipeptidase;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:9751644}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 21,213
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.4 mM for D-Ala-D-Ala {ECO:0000269|PubMed:9751644}; KM=550 mM for L-Ala-D-Ala {ECO:0000269|PubMed:9751644}; Note=kcat is 170 sec(-1) with D-Ala-D-Ala. kcat is 70 sec(-1) with L-Ala-D-Ala.;
Metal Binding METAL 98; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01924; METAL 105; /note=Zinc; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01924; METAL 165; /note=Zinc; via pros nitrogen; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01924
Rhea ID RHEA:20661
Cross Reference Brenda