Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

1.21.4.2: glycine reductase

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

Word Map on EC 1.21.4.2

Reaction

acetyl phosphate
+
NH3
 +
thioredoxin disulfide
 +
H2O
=
glycine
 +
phosphate
 +
thioredoxin

Synonyms

glycine reductase, GrdA

ECTree

     1 Oxidoreductases
         1.21 Catalysing the reaction X-H + Y-H = X-Y
             1.21.4 With a disulfide as acceptor
                1.21.4.2 glycine reductase

Engineering

Engineering on EC 1.21.4.2 - glycine reductase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C242A
no cleavage on the N-terminal side of a cysteine
C242S
cleavage on the N-terminal side of a cysteine under similar conditions with more extended half-times than wild-type enzyme
C242T
cleavage on the N-terminal side of a cysteine under similar conditions with more extended half-times than wild-type enzyme
C242A
-
no cleavage on the N-terminal side of a cysteine
-
C242S
-
cleavage on the N-terminal side of a cysteine under similar conditions with more extended half-times than wild-type enzyme
-
C242T
-
cleavage on the N-terminal side of a cysteine under similar conditions with more extended half-times than wild-type enzyme
-
C353
-
mutation of potentially redox-active motif UxxCxxC, 44% of wild-type peroxidase activity
C356
-
mutation of potentially redox-active motif UxxCxxC, 40% of wild-type peroxidase activity
C359A
-
grdD of protein component C, mutant enzyme completely inactive, accessible to iodoacetate only under native conditions, suggesting that Cys359 of GrdD is the thiol responsible for the formation of the acetyl thioester during catalysis of arsenate-dependent hydrolysis of acetyl phosphate
C98S
-
grdD of protein component C, activity is unchanged, accessible to iodoacetate only after denaturation
U350
-
mutation of potentially redox-active motif UxxCxxC, 60% of wild-type peroxidase activity
additional information