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4.1.1.82: phosphonopyruvate decarboxylase

This is an abbreviated version!
For detailed information about phosphonopyruvate decarboxylase, go to the full flat file.

Word Map on EC 4.1.1.82

Reaction

3-phosphonopyruvate
=
2-phosphonoacetaldehyde
 +
CO2

Synonyms

PnPy decarboxylase, Ppd, PPDC, Ppyr decarboxylase

ECTree

     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.82 phosphonopyruvate decarboxylase

Engineering

Engineering on EC 4.1.1.82 - phosphonopyruvate decarboxylase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D258A
9% of wild-type kcat for 3-phosphonopyruvate
D260A
0.1% of wild-type kcat for 3-phosphonopyruvate
E213A
5% of wild-type kcat for 3-phosphonopyruvate
D297E
catalytic turnover rate is 1.5fold less and Km is increased about 13fold compared to the wild type enzyme
D297N
catalytic turnover rate of D297N is 2fold lower and Km is increased 940fold compared to the wild type enzyme
G94A
compared to wild type PPDC, Km is increased only 2fold, while kcat is 4fold lower
H110A
no detectable activity
H111A
the mutation has no significant influence on the steady state kinetic constants compared to the wild type enzyme
S25D
catalytic turnover rate is 4fold less and Km is increased 460fold compared to the wild type enzyme
S25N
catalytic turnover rate is 1.5fold less and Km is increased 80fold compared to the wild type enzyme
D297N
Streptomyces viridochromogenes DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494 / Tu 494
-
catalytic turnover rate of D297N is 2fold lower and Km is increased 940fold compared to the wild type enzyme
-
G94A
Streptomyces viridochromogenes DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494 / Tu 494
-
compared to wild type PPDC, Km is increased only 2fold, while kcat is 4fold lower
-
H110A
Streptomyces viridochromogenes DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494 / Tu 494
-
no detectable activity
-
H111A
Streptomyces viridochromogenes DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494 / Tu 494
-
the mutation has no significant influence on the steady state kinetic constants compared to the wild type enzyme
-
S25D
Streptomyces viridochromogenes DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494 / Tu 494
-
catalytic turnover rate is 4fold less and Km is increased 460fold compared to the wild type enzyme
-