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1.3.1.33: protochlorophyllide reductase

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

Word Map on EC 1.3.1.33

Reaction

chlorophyllide a
+
NADP+
=
protochlorophyllide
 +
NADPH
 +
H+

Synonyms

3PCR, B9Z40_03660, bchB, bchL, bchN, dark active protochlorophyllide oxidoreductase, dark operative protochlorophyllide oxidoreductase, dark-operative protochlorophyllide oxidoreductase, DPOR, EH32_03160, faded green leaf, Fgl, GEMMAAP_15250, LHPP, light-activated enzyme protochlorophyllide oxidoreductase, light-dependent NADPH-protochlorophyllide oxidoreductase, light-dependent NADPH: protochlorophyllide oxidoreductase, light-dependent NADPH:Pchlide oxidoreductase, light-dependent NADPH:protochlorophyllide oxidoreductase, light-dependent Pchlide oxidoreductase, Light-dependent protochlorophyllide oxidoreductase, light-driven enzyme protochlorophyllide oxidoreductase, light-independent (dark) Pchlide oxidoreductase, light-independent NADPH:protochlorophyllide oxidoreductase, light-independent protochlorophyllide oxidoreductase, LIPOR, LPOR, NADPH Pchlide oxidoreductase, NADPH-Pchlide oxidoreductase, NADPH-protochlorophyllide oxidoreductase, NADPH-protochlorophyllide oxidoreductase (POR)-like protein, NADPH-protochlorophyllide oxidoreductase A, NADPH-protochlorophyllide oxidoreductase B, NADPH-protochlorophyllide reductase, NADPH2-protochlorophyllide oxidoreductase, NADPH: protochlorophyllide oxidoreductase, NADPH: protochlorophyllide oxidoreductase A, NADPH: protochlorophyllide oxidoreductase B, NADPH:Pchlide oxidoreductase, NADPH:Pchlide oxidoreductase A, NADPH:protochlorophyllide (Pchlide) oxidoreductase, NADPH:protochlorophyllide oxidoreductase, NADPH:protochlorophyllide oxidoreductase A, NADPH:protochlorophyllide oxidoreductase B, Os04g58200, Os10g0496900, OsPORA, OsPORB, PAR-A, Pchilde reductase, Pchlide oxidoreductase, PCR, POR, POR A, POR B, POR C, POR pPm1, POR pPm2, POR-A, POR-B, POR-C, POR-PChlide640, POR-PChlide650, POR1, POR2, POR3, PORA, PORB, PORC, protochlorophyllide oxidoreductase, protochlorophyllide oxidoreductase A, protochlorophyllide oxidoreductase B, protochlorophyllide oxidoreductase C, protochlorophyllide oxidoreductase POR-PChlide640, protochlorophyllide oxidoreductase POR-PChlide650, protochlorophyllide photooxidoreductase, protochlorophyllide reductase

ECTree

     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.1 With NAD+ or NADP+ as acceptor
                1.3.1.33 protochlorophyllide reductase

Engineering

Engineering on EC 1.3.1.33 - protochlorophyllide reductase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C276A
-
the mutant is hypersensitive to high-light conditions during greening
Cys303A
-
the mutant is hypersensitive to high-light conditions during greening
R321A
-
inactive
T316A/T317A
-
inactive
C103S
-
the BchN subunit variant shows 0.5% residual activity and is essentially inactive
C21S
-
the BchN subunit variant shows 0.5% residual activity and is essentially inactive
C46S
-
the BchN subunit variant shows 0.5% residual activity and is essentially inactive
C104A
-
no detectable effect on the import of protein to plastid and processing in darkness
C166A
-
no detectable effect on the import of protein to plastid and processing in darkness
C195A
-
mutant, constructed for the identification of the protochlorophyllide binding site
C222A
-
mutant, constructed for the identification of the protochlorophyllide binding site
C276A
-
decrease in mature enzyme protein present in plastid and decrease in the amount of protochlorophyllide bound to enzyme. C276 constitutes the protochlorophyllide binding site in the active centre of enzyme
C303A
-
decrease in mature enzyme protein present in plastid and decrease in the amount of protochlorophyllide bound to enzyme. C303 constitutes a low affinity protochlorophyllide binding site involved in assembly and stabilization of imported enzyme inside etioplasts
C33A
-
mutant, constructed for the identification of the protochlorophyllide binding site
C85A
-
mutant, constructed for the identification of the protochlorophyllide binding site
H394A
mutant retains only a moderate activity which points to a critical role of this residue in the specific protonation at C-18, probably by positioning a water molecule at a distance of 3.2 A from C-18 above the ring
Y189F
-
mutant, the putative proton donor, Tyr 189, is replaced by a phenylalanine residue
C199/C226S
Thermosynechococcus vestitus
-
mutant, mutation of the absolutely conserved cysteine residues
C199S
C199S/C226S
Thermosynechococcus vestitus
-
kcat more that 10fold decreased to wild-type, relative activity highly decreased compared to wild-type, Kd (NADPH) 2fold increased compared to wild-type, Kd (protochlorophyllide) 6fold increased compared to wild-type
C226S
C37S/C199S
C37S/C199S/C226S
C37S/C226S
F233L
Thermosynechococcus vestitus
-
mutant enzyme shows around 40% of wild-type activity
F233Y
Thermosynechococcus vestitus
-
mutant enzyme shows around 40% of wild-type activity
F237Y
Thermosynechococcus vestitus
-
as in the wild-type enzyme the visible spectrum of protochlorophyllide bound to the mutant enzyme is red-shifted by about 12 nm compared to free protochlorophyllide
F240Y
Thermosynechococcus vestitus
-
distinct from the wild-type enzyme the visible spectrum of protochlorophyllide bound to the mutant enzyme is not red-shifted as compared to free protochlorophyllide
F244Y
Thermosynechococcus vestitus
-
distinct from the wild-type enzyme the visible spectrum of protochlorophyllide bound to the mutant enzyme is not red-shifted as compared to free protochlorophyllide
F247Y
Thermosynechococcus vestitus
-
distinct from the wild-type enzyme the visible spectrum of protochlorophyllide bound to the mutant enzyme is not red-shifted as compared to free protochlorophyllide
G19A
Thermosynechococcus vestitus
the mutant shows wild type value for turnover number
H236A
Thermosynechococcus vestitus
the mutant shows reduced value for turnover number compared to the wild type enzyme
K197A
Thermosynechococcus vestitus
-
mutant, constructed for analysing the role of the conserved active site lysine
K197Q
Thermosynechococcus vestitus
-
mutant, constructed for analysing the role of the conserved active site lysine
K197R
Thermosynechococcus vestitus
-
mutant, constructed for analysing the role of the conserved active site lysine
K42A
Thermosynechococcus vestitus
the mutant shows wild type value for turnover number
N149V
Thermosynechococcus vestitus
the mutant shows reduced value for turnover number compared to the wild type enzyme
N39V
Thermosynechococcus vestitus
the mutant shows reduced value for turnover number compared to the wild type enzyme
N90A
Thermosynechococcus vestitus
the mutant shows reduced value for turnover number compared to the wild type enzyme
R38V
Thermosynechococcus vestitus
the mutant shows wild type value for turnover number
S16C
Thermosynechococcus vestitus
the mutant shows wild type value for turnover number
S189A
Thermosynechococcus vestitus
the mutant shows wild type value for turnover number
T145A
Thermosynechococcus vestitus
the mutant shows reduced value for turnover number compared to the wild type enzyme
T147F
Thermosynechococcus vestitus
the mutant shows reduced value for turnover number compared to the wild type enzyme
T147S
Thermosynechococcus vestitus
the mutant shows reduced value for turnover number compared to the wild type enzyme
T230A
Thermosynechococcus vestitus
the mutant shows wild type value for turnover number
T230F
Thermosynechococcus vestitus
the mutant shows reduced value for turnover number compared to the wild type enzyme
T230S
Thermosynechococcus vestitus
the mutant shows wild type value for turnover number
Y193A
Thermosynechococcus vestitus
-
mutant, constructed for analysing the role of the conserved active site tyrosine
Y193F
Thermosynechococcus vestitus
-
mutant, constructed for analysing the role of the conserved active site tyrosine
Y193S
Thermosynechococcus vestitus
-
mutant, constructed for analysing the role of the conserved active site tyrosine
Y94F
Thermosynechococcus vestitus
the mutant shows wild type value for turnover number