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3.4.14.5: dipeptidyl-peptidase IV

This is an abbreviated version!
For detailed information about dipeptidyl-peptidase IV, go to the full flat file.

Word Map on EC 3.4.14.5

Reaction

release of an N-terminal dipeptide, Xaa-Yaa-/-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline =

Synonyms

(GLP1)-degrading enzyme, ACT3, ADA binding protein, ADA-binding protein, ADABP, adenosine deaminase binding protein, Adenosine deaminase complexing protein, adenosine deaminase-binding protein, amino acyl-prolyl dipeptidyl aminopeptidase, aminopeptidase, glycylproline, Bile canaliculus domain-specific membrane glycoprotein, CD26, CD26 peptidase, CD26/dipeptidyl peptidase, CD26/DP IV, DAP IV, DapB, dapUm, dipeptidyl aminopeptidase IV, dipeptidyl dipeptidase IV, dipeptidyl peptidase 4, dipeptidyl peptidase 8, dipeptidyl peptidase 9, dipeptidyl peptidase IV, dipeptidyl peptidase-4, dipeptidyl peptidase-IV, dipeptidyl-aminopeptidase IV, dipeptidyl-peptidase 4, dipeptidyl-peptidase IV (CD26), dipeptidyl-peptide hydrolase, dipeptidylpeptidase 4a, dipeptidylpeptidase 4b, dipeptidylpeptidase IV, dipeptidylpeptidase IV/CD26, dipeptidylpeptidase-IV, DP IV, DP-IV, DPIV, DPP, DPP IV, DPP IV/CD26, DPP-4, DPP-IV, DPP4, DPP8, DPP9, DPPIV, DppIVA, DppIVB, glucagon-like peptide 1-degrading enzyme, Gly-Pro-naphthylamidase, glycoprotein GP110, glycylproline aminopeptidase, glycylproline-dipeptidyl-aminopeptidase, glycylprolyl aminopeptidase, glycylprolyl dipeptidylaminopeptidase, GP110 glycoprotein, h-DPPIV, hDPPIV, leukocyte antigen CD26, lymphocyte, antigen CD26, More, omega DPPIV, omega enzyme, omega gene product, Pep X, peptidase, dipeptidyl, IV, PepX, postproline dipeptidyl aminopeptidase IV, prolyl-dipeptidyl-aminopeptidase, sipeptidyl peptidase IV, T cell triggering molecule Tp103, T-cell activation antigen CD26, THAM, Thymocyte-activating molecule, TP103, type IV dipeptidyl aminopeptidase, WC10, X-PDAP, X-prolyl dipeptidyl aminopeptidase, X-prolyl-dipeptidyl aminopeptidase, Xaa-Pro-dipeptidyl-aminopeptidase

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.14 Dipeptidyl-peptidases and tripeptidyl-peptidases
                3.4.14.5 dipeptidyl-peptidase IV

Engineering

Engineering on EC 3.4.14.5 - dipeptidyl-peptidase IV

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D708A
mutant enzyme shows less than 1% of wild-type activity
F713A
mutation disrupts dimeric DPP-IV into monomers. kcat/Km for Gly-Pro-p-nitroaniline is 27fold lower wild-type value
F730A
mutant enzyme is a mixture of monomers and dimers. With the dimeric mutant enzyme the kcat/Km for Gly-Pro-p-nitroaniline is 1.9fold lower than wild-type value. With the monomeric mutant enzyme the kcat/Km for Gly-Pro-p-nitroaniline is 241fold lower than wild-type value
F822A
-
the DPP8 mutation abolishes the enzymatic activity without disrupting its quaternary structure
F842A
-
the DPP9 mutation abolishes the enzymatic activity without disrupting its quaternary structure
H740L
mutant enzyme shows less than 1% of wild-type activity
N150A
N219A
N229A
N281A
N321A
N520A
N685A
S630A
mutant enzyme shows less than 1% of wild-type activity
V724A
mutant enzyme remains largely dimeric. With the dimeric mutant enzyme the kcat/Km for Gly-Pro-p-nitroaniline is 1.8fold lower than wild-type value. With the monomeric mutant enzyme the kcat/Km for Gly-Pro-p-nitroaniline is 138fold lower than wild-type value
W734A
mutation disrupts dimeric DPP-IV into monomers with a small fraction of dimers. With the monomeric mutant enzyme the kcat/Km for Gly-Pro-p-nitroaniline is 322fold lower than wild-type value
Y547F
mutant enzyme shows less than 1% of wild-type activity, kcat/Km is 1523fold lower than wild-type value
Y735A
mutation disrupts dimeric DPP-IV into monomers. With the monomeric mutant enzyme the kcat/Km for Gly-Pro-p-nitroaniline is 1612fold lower than wild-type value
D702A
-
no hydrolyis of Gly-Pro-4-nitroanilide
D702E
-
no hydrolyis of Gly-Pro-4-nitroanilide
H734L
-
no hydrolyis of Gly-Pro-4-nitroanilide
H734R
-
no hydrolyis of Gly-Pro-4-nitroanilide
S624A
-
no hydrolyis of Gly-Pro-4-nitroanilide
S624T
-
no hydrolysis of Gly-Pro-4-nitroanilide
D702A
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
H743A
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
S624A
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
C299G
site-directed mutagenesis, similar to the wild-type enzyme
C326G
site-directed mutagenesis, total inhibition of surface expression, catalytically inactive, half-life of the mutant enzyme is reduced by over 90%
C337S
site-directed mutagenesis, weak expression, reduced activity, half-life of the mutant enzyme is reduced by over 90%
C383G
site-directed mutagenesis, similar to the wild-type enzyme
C395S
site-directed mutagenesis, similar to the wild-type enzyme
C445S
site-directed mutagenesis, total inhibition of surface expression, catalytically inactive, half-life of the mutant enzyme is reduced by over 90%
C448S
site-directed mutagenesis, total inhibition of surface expression, catalytically inactive, half-life of the mutant enzyme is reduced by over 90%
C455G
site-directed mutagenesis, weak expression, reduced activity, half-life of the mutant enzyme is reduced by over 90%
C473S
site-directed mutagenesis, weak expression, reduced activity, half-life of the mutant enzyme is reduced by over 90%
C552S
site-directed mutagenesis, weak expression, reduced activity, half-life of the mutant enzyme is reduced by over 90%
C650G
site-directed mutagenesis, similar to the wild-type enzyme
C763S
site-directed mutagenesis, similar to the wild-type enzyme
G629X
-
complete loss of activity
G633X
-
complete loss of activity
S631X
-
complete loss of activity
additional information