Detail Information for IndEnz0002018884
IED ID IndEnz0002018884
Enzyme Type ID protease018884
Protein Name D-aminopeptidase
EC 3.4.11.19
Gene Name dap GOX1238
Organism Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Alphaproteobacteria Rhodospirillales Acetobacteraceae Gluconobacter Gluconobacter oxydans (Gluconobacter suboxydans) Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans)
Enzyme Sequence MSDSFSARLEAAVSALPARFPGPGGAVAVLKDGEVLVRHGWGYANVERRIPFTPSTLFRMCSITKQFTCGTLLDLYDDPSELDADVDARLPQLDEPSPGMLHLAHNQSGLRDYWAVAMLHGAPIEGYFGDREARRVIDGTRTLQFQPGTSYSYVNQNFRLISDILQDRTGRSFAELLQTSIFNPVGMERAILAAETRAMPDGTVGYEGSVESGFRPAINNIWWTGDAGLGASLDDMIAWERFIDETRDAPDSLYRRLTVPVTFSDGQPAPYGFGLQRTKMFGRDVTMHGGALRGWRSHRLHVASERLSVVVMFNHMSAAQVASAQILAAALGVPYEPERSTQQPTALYGTYLERETGLSARIEPAPGGAKLRYLMVPELLEGISATRAEAGSVVVKAQETAEGAEAVMERPGENRTSILARCDETPGEDIAELAGVYRCEELDEAEVTIELAGGVVYGGFSGILGDGRMEMLQRLAKDVWVLPCPRALDHTAPGDWTLAFERQGGSVTAVRVGCWLARDLMYQRV
Enzyme Length 525
Uniprot Accession Number Q5FRJ7
Absorption
Active Site ACT_SITE 62; /note=Nucleophile; /evidence=ECO:0000255|HAMAP-Rule:MF_01960; ACT_SITE 65; /note=Proton donor/acceptor; /evidence=ECO:0000255|HAMAP-Rule:MF_01960
Activity Regulation ACTIVITY REGULATION: Inhibited by beta-lactam compounds such as 6-aminopenicillic acid, 7-aminocephalosporanic acid, benzylpenicillin and ampicillin. Inhibited by p-chloromercuribenzoate. {ECO:0000255|HAMAP-Rule:MF_01960}.
Binding Site BINDING 489; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_01960
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Release of an N-terminal D-amino acid from a peptide, Xaa-|-Yaa-, in which Xaa is preferably D-Ala, D-Ser or D-Thr. D-amino acid amides and methyl esters also are hydrolyzed, as is glycine amide.; EC=3.4.11.19; Evidence={ECO:0000255|HAMAP-Rule:MF_01960};
DNA Binding
EC Number 3.4.11.19
Enzyme Function FUNCTION: Hydrolyzes N-terminal residues in D-amino acid-containing peptides. {ECO:0000255|HAMAP-Rule:MF_01960}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Binding site (1); Chain (1); Region (1)
Keywords Aminopeptidase;Hydrolase;Protease;Reference proteome
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 57,398
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda