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

BRENDA support

Literature summary for 1.3.1.33 extracted from

  • Yamamoto, H.; Kojima-Ando, H.; Ohki, K.; Fujita, Y.
    Formation of prolamellar-body-like ultrastructures in etiolated cyanobacterial cells overexpressing light-dependent protochlorophyllide oxidoreductase in Leptolyngbya boryana (2020), J. Gen. Appl. Microbiol., 66, 129-139 .
    View publication on PubMed
Search for more literature for 1.3.1.33

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli with a Strep-tag Leptolyngbya boryana

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0078
-
 protochlorophyllide pH 7.5, 30°C Leptolyngbya boryana
0.0085
-
 NADPH pH 7.5, 30°C Leptolyngbya boryana

Localization

Localization Comment Organism GeneOntology No. Textmining
etioplast the enzyme (LPOR) exists as a ternary complex of protochlorophyllidee-NADPH-LPOR to form paracrystalline prolamellar bodies (PLBs) in etioplasts Leptolyngbya boryana 9513
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
protochlorophyllide + NADPH + H+ Leptolyngbya boryana
-
 chlorophyllide a + NADP+
-
 ?
protochlorophyllide + NADPH + H+ Leptolyngbya boryana dg5
-
 chlorophyllide a + NADP+
-
 ?

Organism

Organism UniProt Comment Textmining
Leptolyngbya boryana O66148
-
-
Leptolyngbya boryana dg5 O66148
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
protochlorophyllide + NADPH + H+
-
 Leptolyngbya boryana chlorophyllide a + NADP+
-
 ?
protochlorophyllide + NADPH + H+
-
 Leptolyngbya boryana dg5 chlorophyllide a + NADP+
-
 ?

Synonyms

Synonyms Comment Organism
light-dependent Pchlide oxidoreductase
-
 Leptolyngbya boryana
LPOR
-
 Leptolyngbya boryana

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Leptolyngbya boryana

General Information

General Information Comment Organism
physiological function the enzyme (LPOR) exhibits an intrinsic ability to form prolamellar body-like ultrastructures in the presence of the co-accumulation of protochlorophyllide. However, the prolamellar body-like structure differs from the authentic prolamellar bodies regarding NADPH deficiency Leptolyngbya boryana