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Information on EC 1.1.1.327 - 5-exo-hydroxycamphor dehydrogenase
for references in articles please use BRENDA:EC1.1.1.327
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.327 5-exo-hydroxycamphor dehydrogenase
IUBMB Comments
Contains Zn2+. Isolated from Pseudomonas putida, and involved in degradation of (+)-camphor.
The expected taxonomic range for this enzyme is: Bacteria, Archaea
showSynonyms
5-exo-hydroxycamphor dehydrogenase, 5-exo-alcohol dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5-exo-alcohol dehydrogenase
camD
F-dehydrogenase
-
-
-
-
FdeH
FdeH
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5-exo-hydroxycamphor + NAD+ = bornane-2,5-dione + NADH + H+
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
5-exo-hydroxycamphor:NAD+ oxidoreductase
Contains Zn2+. Isolated from Pseudomonas putida, and involved in degradation of (+)-camphor.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5-exo-hydroxycamphor + NAD+
bornane-2,5-dione + NADH + H+
Substrates: -
Products: -
Products: -
r
bornane-2,5-dione + NADH + H+
5-exo-hydroxycamphor + NAD+
Substrates: -
Products: -
Products: -
r
additional information
?
-
Substrates: no substrate: camphor
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
two firmly bound zinc atoms per subunit. All three ligands, C40, H62 and C158 to the catalytic zinc atom in the active-site, and all four ligands, C98, C101, C104 and Cll2 to the second zinc atom, are conserved
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
sequence shows one nucleotide exchange at position 336, at which replacement of a guanine by a cytosine takes place
UniProt
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
Pseudomonas putida PpGl, which carries the CAM plasmid encoding enzymes involved in the degradation pathway of D-camphor, can utilize D-camphor as a sole carbon source. The enzymes responsible for early steps in D-camphor degradation are 5-exo-hydroxycamphor dehydrogenase (camD gene), cytochrome P-450cam (camC), NADH-putidaredoxin reductase (camA), and putidaredoxin (camB)
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A1Q9P026_9ARCH
363
0
39810
TrEMBL
-
A0A1V6FH96_9BACT
368
0
39110
TrEMBL
-
A0A1V5M6L5_9BACT
212
0
22632
TrEMBL
-
A0A1V5DUA7_9DELT
371
0
40359
TrEMBL
-
A0A1S1H838_9SPHN
362
0
38237
TrEMBL
-
A0A1Q9P8G1_THOAA
Thorarchaeota archaeon (strain AB_25)
370
0
40092
TrEMBL
-
K5BFM4_MYCHD
Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849)
377
0
40376
TrEMBL
-
A0A1V5ECK3_9DELT
364
0
39791
TrEMBL
-
A0A1Q9NG85_HEILC
Heimdallarchaeota archaeon (strain LC_2)
363
0
40015
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
gene camD encoding 5-exo-hydroxycamphor dehydrogenase is plasmid born, cotransferable by conjugation, mitomycin curable, and shows a higher segregation rate from cells that are multiplasmid rather than carrying a single plasmid
-
the genes of the CAM plasmid encoding enzymes involved in the degradation pathway of D-camphor form an operon, camDCAB, and are under negative control by the gene camR located immediately upstream from the camD gene
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthetic route for the synthesis of bifunctional camphor derivatives. The combination of the enzymatic P450cam system with 5-exo-hydroxycamphor dehydrogenase (FdeH) allows an efficient synthesis of 2,5-diketobornane, which can be used for further derivatisation
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Aramaki, H.; Koga, H.; Sagara, Y.; Hosoi, M.; Horiuchi, T.
Complete nucleotide sequence of the 5-exo-hydroxycamphor dehydrogenase gene on the CAM plasmid of Pseudomonas putida (ATCC 17453)
Biochim. Biophys. Acta
1174
91-94
1993
Pseudomonas putida (P09347), Pseudomonas putida, Pseudomonas putida ATCC 17453 (P09347)
brenda
Koga, H.; Yamaguchi, E.; Matsunaga, K.; Aramaki, H.; Horiuchi, T.
Cloning and nucleotide sequences of NADH-putidaredoxin reductase gene (camA) and putidaredoxin gene (camB) involved in cytochrome P-450cam hydroxylase of Pseudomonas putida
J. Biochem.
106
831-836
1989
Pseudomonas putida (P09347), Pseudomonas putida
brenda
Rheinwald, J.; Chakrabarty, A.; Gunsalus, I.
A transmissible plasmid controlling camphor oxidation in Pseudomonas putida
Proc. Natl. Acad. Sci. USA
70
885-889
1973
Pseudomonas putida
brenda
Hofer, M.; Strittmatter, H.; Sieber, V.
Biocatalytic synthesis of a diketobornane as a building block for bifunctional camphor derivatives
ChemCatChem
5
3351-3357
2013
Pseudomonas putida (P09347)
-
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.327)
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Release 2023.1 (January 2023)
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