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Information on EC 1.1.1.396 - bacteriochlorophyllide a dehydrogenase
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1.1.1.396 bacteriochlorophyllide a dehydrogenaseIUBMB Comments
The enzyme, together with EC 1.3.7.15, chlorophyllide-a reductase, and EC 4.2.1.165, chlorophyllide-a 31-hydratase, is involved in the conversion of chlorophyllide a to bacteriochlorophyllide a. The enzymes can act in multiple orders, resulting in the formation of different intermediates, but the final product of the cumulative action of the three enzymes is always bacteriochlorophyllide a. The enzyme oxidizes a hydroxyl group on ring A, converting it to an oxo group.
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide a dehydrogenase, bchc oxidoreductase, 3-hydroxyethyl bacteriochlorophyllide a dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide a dehydrogenase
3-hydroxyethyl bacteriochlorophyllide a dehydrogenase
bchC
BchC oxidoreductase
oxidoreductase BchC
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide a dehydrogenase
-
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide a dehydrogenase
Cereibacter sphaeroides NCIB 8253
-
-
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide a dehydrogenase
-
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide a dehydrogenase
-
-
bchC
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a + NAD+ = bacteriochlorophyllide a + NADH + H+
(1)
-
-
-
3-devinyl-3-(1-hydroxyethyl)chlorophyllide a + NAD+ = 3-acetyl-3-devinylchlorophyllide a + NADH + H+
(2)
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
,
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SYSTEMATIC NAME
IUBMB Comments
3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide-a:NAD+ oxidoreductase (bacteriochlorophyllide a-forming)
The enzyme, together with EC 1.3.7.15, chlorophyllide-a reductase, and EC 4.2.1.165, chlorophyllide-a 31-hydratase, is involved in the conversion of chlorophyllide a to bacteriochlorophyllide a. The enzymes can act in multiple orders, resulting in the formation of different intermediates, but the final product of the cumulative action of the three enzymes is always bacteriochlorophyllide a. The enzyme oxidizes a hydroxyl group on ring A, converting it to an oxo group.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-devinyl-2-(1-hydroxyethyl)chlorophyllide a + NAD+
2-acetyl-2-devinylchlorophyllide a + NADH + H+
3(1)R-3-(1-hydroxyethyl)-bacteriochlorophyllide a + NAD+
bacteriochlorophyllide a + NADH + H+
3-(hydroxy)ethyl-13-hydroxy-pheophorbide a + NAD+
3-acetyl-13-hydroxy-pheophorbide a + NADH + H+
3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a + NAD+
bacteriochlorophyllide a + NADH + H+
3-devinyl-3-(1-hydroxyethyl)chlorophyllide a + NAD+
3-acetyl-3-devinylchlorophyllide a + NADH + H+
31R-3-(1-hydroxyethyl)-bacteriochlorophyllide a + NAD+
bacteriochlorophyllide a + NADH + H+
bacteriochlorophyllide a + NADH + H+
3(1)R-3-(1-hydroxyethyl)-bacteriochlorophyllide a + NAD+
zinc 3-(1-hydroxyethyl)-pheophorbide + NAD+
zinc 3-acetyl-(1-hydroxyethyl)-pheophorbide + NADH + H+
2-devinyl-2-(1-hydroxyethyl)chlorophyllide a + NAD+
2-acetyl-2-devinylchlorophyllide a + NADH + H+
-
-
-
?
2-devinyl-2-(1-hydroxyethyl)chlorophyllide a + NAD+
2-acetyl-2-devinylchlorophyllide a + NADH + H+
Cereibacter sphaeroides NCIB 8253
-
-
-
?
3(1)R-3-(1-hydroxyethyl)-bacteriochlorophyllide a + NAD+
bacteriochlorophyllide a + NADH + H+
-
-
-
r
3(1)R-3-(1-hydroxyethyl)-bacteriochlorophyllide a + NAD+
bacteriochlorophyllide a + NADH + H+
-
-
-
-
r
3(1)R-3-(1-hydroxyethyl)-chlorophyllide a + NAD+
3-acetylchlorophyllide a + NADH + H+
-
-
-
r
3(1)R-3-(1-hydroxyethyl)-chlorophyllide a + NAD+
3-acetylchlorophyllide a + NADH + H+
-
-
-
-
r
3-(hydroxy)ethyl-13-hydroxy-pheophorbide a + NAD+
3-acetyl-13-hydroxy-pheophorbide a + NADH + H+
-
-
-
?
3-(hydroxy)ethyl-13-hydroxy-pheophorbide a + NAD+
3-acetyl-13-hydroxy-pheophorbide a + NADH + H+
-
-
-
?
3-acetylchlorophyllide a + NADH + H+
3(1)R-3-(1-hydroxyethyl)-chlorophyllide a + NAD+
-
-
-
r
3-acetylchlorophyllide a + NADH + H+
3(1)R-3-(1-hydroxyethyl)-chlorophyllide a + NAD+
-
-
-
-
r
3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a + NAD+
bacteriochlorophyllide a + NADH + H+
-
-
-
?
3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a + NAD+
bacteriochlorophyllide a + NADH + H+
Cereibacter sphaeroides NCIB 8253
-
-
-
?
3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a + NAD+
bacteriochlorophyllide a + NADH + H+
-
-
-
?
3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a + NAD+
bacteriochlorophyllide a + NADH + H+
-
-
-
?
3-devinyl-3-(1-hydroxyethyl)chlorophyllide a + NAD+
3-acetyl-3-devinylchlorophyllide a + NADH + H+
-
-
-
?
3-devinyl-3-(1-hydroxyethyl)chlorophyllide a + NAD+
3-acetyl-3-devinylchlorophyllide a + NADH + H+
-
-
-
?
3-hydroxyethyl chlorophyllide a + NAD+
bacteriopheophorbide a + NADH + H+
-
-
-
?
3-hydroxyethyl chlorophyllide a + NAD+
bacteriopheophorbide a + NADH + H+
-
-
-
?
31R-3-(1-hydroxyethyl)-bacteriochlorophyllide a + NAD+
bacteriochlorophyllide a + NADH + H+
-
-
-
?
31R-3-(1-hydroxyethyl)-bacteriochlorophyllide a + NAD+
bacteriochlorophyllide a + NADH + H+
-
-
-
-
?
31R-3-(1-hydroxyethyl)-chlorophyllide a + NAD+
3-acetylchlorophyllide a + NADH + H+
-
-
-
?
31R-3-(1-hydroxyethyl)-chlorophyllide a + NAD+
3-acetylchlorophyllide a + NADH + H+
-
-
-
-
?
bacteriochlorophyllide a + NADH + H+
3(1)R-3-(1-hydroxyethyl)-bacteriochlorophyllide a + NAD+
-
-
-
r
bacteriochlorophyllide a + NADH + H+
3(1)R-3-(1-hydroxyethyl)-bacteriochlorophyllide a + NAD+
-
-
-
-
r
bacteriopheophorbide a + NAD+
3-hydroxyethyl-bacteriopheophorbide a + NADH + H+
-
-
-
?
bacteriopheophorbide a + NAD+
3-hydroxyethyl-bacteriopheophorbide a + NADH + H+
-
-
-
?
zinc 3-(1-hydroxyethyl)-pheophorbide + NAD+
zinc 3-acetyl-(1-hydroxyethyl)-pheophorbide + NADH + H+
the R-epimer is consumed as a substrate to a greater extent than is the S-epimer. The R-epimer is consumed as a substrate in the reverse reaction to a greater extent than is the S-epimer
-
-
r
zinc 3-(1-hydroxyethyl)-pheophorbide + NAD+
zinc 3-acetyl-(1-hydroxyethyl)-pheophorbide + NADH + H+
-
the R-epimer is consumed as a substrate to a greater extent than is the S-epimer. The R-epimer is consumed as a substrate in the reverse reaction to a greater extent than is the S-epimer
-
-
r
additional information
?
-
no activity with 3-hydroxyethyl-bacteriochlorophyll a
-
-
?
additional information
?
-
-
no activity with 3-hydroxyethyl-bacteriochlorophyll a
-
-
?
additional information
?
-
-
BchC preferentially oxidizes 31R-3-(1-hydroxyethyl)-chlorophyllide a and 31R-3-(1-hydroxyethyl)-bacteriochlorophyllide a in the presence of NAD+ to 3-acetylchlorophyllide a and bacteriochlorophyllide a, respectively, leaving the unreacted 31S-epimers. In the reverse reaction, BchC with NADH predominately produces 31R-epimeric alcohols from the 3-acetyl-(bacterio)chlorins. 31R-selectivity, overview. While most naturally occurring (B)Chls including BChl a have a magnesium ion at the center of the cyclic tetrapyrrole ring, zinc-chelated BChl a has been found in some organisms. BchC exhibits oxidation activity on zinc 3-(1-hydroxyethyl)-pheophorbide (Zn-3HE-Pheide) a, albeit at a low level, where the R-epimer is consumed as a substrate to a greater extent than is the S-epimer. The reduction of Zn-3Ac-Pheide a by BchC in the presence of NADH is also observed, predominantly producing the R-epimer of Zn-3HE-Pheide a. The chlorin pigments lacking a central metal, 3HE-Pheide a and 3Ac-Pheide a, are not suitable for substrates of BchC in the presence of NAD+ or NADH, respectively. Thus, the central metal atoms, Mg and Zn, in the substrates are necessary for BchC-catalyzed reaction. Determination of the 31-stereochemistry of 3HEChlide a and 3HE-BChlide a, overview
-
-
-
additional information
?
-
BchC preferentially oxidizes 31R-3-(1-hydroxyethyl)-chlorophyllide a and 31R-3-(1-hydroxyethyl)-bacteriochlorophyllide a in the presence of NAD+ to 3-acetylchlorophyllide a and bacteriochlorophyllide a, respectively, leaving the unreacted 31S-epimers. In the reverse reaction, BchC with NADH predominately produces 31R-epimeric alcohols from the 3-acetyl-(bacterio)chlorins. 31R-selectivity, overview. While most naturally occurring (B)Chls including BChl a have a magnesium ion at the center of the cyclic tetrapyrrole ring, zinc-chelated BChl a has been found in some organisms. BchC exhibits oxidation activity on zinc 3-(1-hydroxyethyl)-pheophorbide (Zn-3HE-Pheide) a, albeit at a low level, where the R-epimer is consumed as a substrate to a greater extent than is the S-epimer. The reduction of Zn-3Ac-Pheide a by BchC in the presence of NADH is also observed, predominantly producing the R-epimer of Zn-3HE-Pheide a. The chlorin pigments lacking a central metal, 3HE-Pheide a and 3Ac-Pheide a, are not suitable for substrates of BchC in the presence of NAD+ or NADH, respectively. Thus, the central metal atoms, Mg and Zn, in the substrates are necessary for BchC-catalyzed reaction. Determination of the 31-stereochemistry of 3HEChlide a and 3HE-BChlide a, overview
-
-
-
additional information
?
-
no activity with 3-hydroxyethyl-bacteriochlorophyll a
-
-
?
additional information
?
-
-
BchC preferentially oxidizes 31R-3-(1-hydroxyethyl)-chlorophyllide a and 31R-3-(1-hydroxyethyl)-bacteriochlorophyllide a in the presence of NAD+ to 3-acetylchlorophyllide a and bacteriochlorophyllide a, respectively, leaving the unreacted 31S-epimers. The enzyme catalyzes both the oxidation of 3HE to 3Ac and the reduction of 3Ac to 3HE, the reverse reaction. In the reverse reaction, BchC with NADH predominately produces 31R-epimeric alcohols from the 3-acetyl-(bacterio)chlorins. 31R-selectivity, overview. While most naturally occurring (B)Chls including BChl a have a magnesium ion at the center of the cyclic tetrapyrrole ring, zinc-chelated BChl a has been found in some organisms. BchC exhibits oxidation activity on zinc 3-(1-hydroxyethyl)-pheophorbide (Zn-3HE-Pheide) a, albeit at a low level, where the R-epimer is consumed as a substrate to a greater extent than is the S-epimer. The reduction of Zn-3Ac-Pheide a by BchC in the presence of NADH is also observed, predominantly producing the R-epimer of Zn-3HE-Pheide a. The chlorin pigments lacking a central metal, 3HE-Pheide a and 3Ac-Pheide a, are not suitable for substrates of BchC in the presence of NAD+ or NADH, respectively. Thus, the central metal atoms, Mg and Zn, in the substrates are necessary for BchC-catalyzed reaction. Determination of the 31-stereochemistry of 3HEChlide a and 3HE-BChlide a, overview
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-devinyl-2-(1-hydroxyethyl)chlorophyllide a + NAD+
2-acetyl-2-devinylchlorophyllide a + NADH + H+
3-(hydroxy)ethyl-13-hydroxy-pheophorbide a + NAD+
3-acetyl-13-hydroxy-pheophorbide a + NADH + H+
3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a + NAD+
bacteriochlorophyllide a + NADH + H+
3-devinyl-3-(1-hydroxyethyl)chlorophyllide a + NAD+
3-acetyl-3-devinylchlorophyllide a + NADH + H+
31R-3-(1-hydroxyethyl)-bacteriochlorophyllide a + NAD+
bacteriochlorophyllide a + NADH + H+
2-devinyl-2-(1-hydroxyethyl)chlorophyllide a + NAD+
2-acetyl-2-devinylchlorophyllide a + NADH + H+
-
-
-
?
2-devinyl-2-(1-hydroxyethyl)chlorophyllide a + NAD+
2-acetyl-2-devinylchlorophyllide a + NADH + H+
Cereibacter sphaeroides NCIB 8253
-
-
-
?
3-(hydroxy)ethyl-13-hydroxy-pheophorbide a + NAD+
3-acetyl-13-hydroxy-pheophorbide a + NADH + H+
-
-
-
?
3-(hydroxy)ethyl-13-hydroxy-pheophorbide a + NAD+
3-acetyl-13-hydroxy-pheophorbide a + NADH + H+
-
-
-
?
3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a + NAD+
bacteriochlorophyllide a + NADH + H+
-
-
-
?
3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a + NAD+
bacteriochlorophyllide a + NADH + H+
Cereibacter sphaeroides NCIB 8253
-
-
-
?
3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a + NAD+
bacteriochlorophyllide a + NADH + H+
-
-
-
?
3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a + NAD+
bacteriochlorophyllide a + NADH + H+
-
-
-
?
3-devinyl-3-(1-hydroxyethyl)chlorophyllide a + NAD+
3-acetyl-3-devinylchlorophyllide a + NADH + H+
-
-
-
?
3-devinyl-3-(1-hydroxyethyl)chlorophyllide a + NAD+
3-acetyl-3-devinylchlorophyllide a + NADH + H+
-
-
-
?
3-hydroxyethyl chlorophyllide a + NAD+
bacteriopheophorbide a + NADH + H+
-
-
-
?
3-hydroxyethyl chlorophyllide a + NAD+
bacteriopheophorbide a + NADH + H+
-
-
-
?
31R-3-(1-hydroxyethyl)-bacteriochlorophyllide a + NAD+
bacteriochlorophyllide a + NADH + H+
-
-
-
?
31R-3-(1-hydroxyethyl)-bacteriochlorophyllide a + NAD+
bacteriochlorophyllide a + NADH + H+
-
-
-
-
?
31R-3-(1-hydroxyethyl)-chlorophyllide a + NAD+
3-acetylchlorophyllide a + NADH + H+
-
-
-
?
31R-3-(1-hydroxyethyl)-chlorophyllide a + NAD+
3-acetylchlorophyllide a + NADH + H+
-
-
-
-
?
bacteriopheophorbide a + NAD+
3-hydroxyethyl-bacteriopheophorbide a + NADH + H+
-
-
-
?
bacteriopheophorbide a + NAD+
3-hydroxyethyl-bacteriopheophorbide a + NADH + H+
-
-
-
?
additional information
?
-
no activity with 3-hydroxyethyl-bacteriochlorophyll a
-
-
?
additional information
?
-
-
no activity with 3-hydroxyethyl-bacteriochlorophyll a
-
-
?
additional information
?
-
no activity with 3-hydroxyethyl-bacteriochlorophyll a
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
BchC protein is a zinc-independent dehydrogenase
additional information
BchC protein is a zinc-independent dehydrogenase
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.8
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
-
BchC oxidoreductase is involved in bacteriochlorophyll a biosynthesis. The presence of BchC accelerates the 3-vinyl hydration by BchF hydratase of Chlorobaculum tepidum during conversion of chlorophyllide a to 3-acetyl-chlorophyllide a through 3-(1-hydroxyethyl)-chlorophyllide a, indicating that these enzymes work cooperatively to promote efficient bacteriochlorophyll a biosynthesis
metabolism
BchC oxidoreductase is involved in bacteriochlorophyll a biosynthesis. The presence of BchC accelerates the 3-vinyl hydration by BchF hydratase of Chlorobaculum tepidum during conversion of chlorophyllide a to 3-acetyl-chlorophyllide a through 3-(1-hydroxyethyl)-chlorophyllide a, indicating that these enzymes work cooperatively to promote efficient bacteriochlorophyll a biosynthesis
metabolism
-
the enzyme is involved in bacteriochlorophyll a biosynthesis
metabolism
the enzyme is involved in bacteriochlorophyll a biosynthesis. The presence of BchC accelerates the 3-vinyl hydration by BchF hydratase of Chlorobaculum tepidum during conversion of chlorophyllide a to 3-acetyl-chlorophyllide a through 3-(1-hydroxyethyl)-chlorophyllide a, indicating that these enzymes work cooperatively to promote efficient bacteriochlorophyll a biosynthesis
physiological function
BchC of Chlorobaculum tepidum preferentially oxidizes porphyrin-type pigments, 31R-3-(1-hydroxyethyl)-chlorophyllide a and 31R-3-(1-hydroxyethyl)-bacteriochlorophyllide a, in the presence of NAD+ to 3-acetylchlorophyllide a and bacteriochlorophyllide a, respectively, leaving the unreacted 31S-epimers. The enzyme catalyzes both the oxidation of 3HE to 3Ac and the reduction of 3Ac to 3HE, the reverse reaction. In the reverse reaction, BchC with NADH predominately produces 31R-epimeric alcohols from the 3-acetyl-(bacterio)chlorins. BchC of Rhodobacter capsulatus demonstrates the same 31R-selectivity, suggesting that utilization of 31R-epimers in BchC-catalyzed reductions may be conserved across different phyla of photosynthetic bacteria
physiological function
-
BchC of Rhodobacter capsulatus preferentially oxidizes porphyrin-type pigments, 31R-3-(1-hydroxyethyl)-chlorophyllide a and 31R-3-(1-hydroxyethyl)-bacteriochlorophyllide a, in the presence of NAD+ to 3-acetylchlorophyllide a and bacteriochlorophyllide a, respectively, leaving the unreacted 31S-epimers. In the reverse reaction, BchC with NADH predominately produces 31R-epimeric alcohols from the 3-acetyl-(bacterio)chlorins. BchC of Chlorobaculum tepidum demonstrates the same 31R-selectivity, suggesting that utilization of 31R-epimers in BchC-catalyzed reductions may be conserved across different phyla of photosynthetic bacteria. The central metal atoms, Mg and Zn, in the substrates are necessary for BchC-catalyzed reaction
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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). BCHC_RHOCB
Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
314
0
33010
Swiss-Prot
-
BCHC_RHOCA
314
0
33010
Swiss-Prot
other Location (Reliability: 3)
BCHC_CERS4
Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.)
318
0
33961
Swiss-Prot
-
Q8KCJ7_CHLTE
Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
337
0
36657
TrEMBL
-
Q93ST5_CHLTP
377
0
40262
TrEMBL
Mitochondrion (Reliability: 4)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant Strep II-tagged enzyme from Escherichia coli
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
gene bciC, recombinant expression of Strep II-tagged enzyme in Escherichia coli strain
gene bciC, recombinant expression of Strep II-tagged enzyme in Escherichia coli strain
-
gene bciC, recombinant expression of Strep II-tagged enzyme in Escherichia coli strain
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
atmospheric oxygen tension (20% 02) reduces the expression of the enzyme compared with low oxygen tension (2% 02)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
McGlynn, P.; Hunter, C.N.
Genetic analysis of the bchC and bchA genes of Rhodobacter sphaeroides
Mol. Gen. Genet.
236
227-234
1993
Cereibacter sphaeroides (Q02430), Cereibacter sphaeroides, Cereibacter sphaeroides NCIB 8253 (Q02430)
brenda
Wellington, C.L.; Beatty, J.T.
Promoter mapping and nucleotide sequence of the bchC bacteriochlorophyll biosynthesis gene from Rhodobacter capsulatus
Gene
83
251-261
1989
Rhodobacter capsulatus (P0CY54), Rhodobacter capsulatus, Rhodobacter capsulatus B10 (P0CY54)
brenda
Biel, A.J.; Marrs, B.L.
Transcriptional regulation of several genes for bacteriochlorophyll biosynthesis in Rhodopseudomonas capsulata in response to oxygen
J. Bacteriol.
156
686-694
1983
Rhodobacter capsulatus (P0CY54)
brenda
Biel, A.J.
Control of bacteriochlorophyll accumulation by light in Rhodobacter capsulatus
J. Bacteriol.
168
655-659
1986
Rhodobacter capsulatus (P0CY54)
brenda
Wellington, C.L.; Taggart, A.K.; Beatty, J.T.
Functional significance of overlapping transcripts of crtEF, bchCA, and puf photosynthesis gene operons in Rhodobacter capsulatus
J. Bacteriol.
173
2954-2961
1991
Rhodobacter capsulatus (P0CY54)
brenda
Penfold, R.J.; Pemberton, J.M.
Sequencing, chromosomal inactivation, and functional expression in Escherichia coli of ppsR, a gene which represses carotenoid and bacteriochlorophyll synthesis in Rhodobacter sphaeroides
J. Bacteriol.
176
2869-2876
1994
Cereibacter sphaeroides (Q02430)
brenda
Ponnampalam, S.N.; Elsen, S.; Bauer, C.E.
Aerobic repression of the Rhodobacter capsulatus bchC promoter involves cooperative interactions between CrtJ bound to neighboring palindromes
J. Biol. Chem.
273
30757-30761
1998
Rhodobacter capsulatus (P0CY54)
brenda
Lange, C.; Kiesel, S.; Peters, S.; Virus, S.; Scheer, H.; Jahn, D.; Moser, J.
Broadened substrate specificity of 3-hydroxyethyl bacteriochlorophyllide a dehydrogenase (BchC) indicates a new route for the biosynthesis of bacteriochlorophyll a
J. Biol. Chem.
290
19697-19709
2015
Chlorobaculum tepidum (Q8KCJ7), Chlorobaculum tepidum, Chlorobaculum tepidum TLS (Q8KCJ7)
brenda
Abada, E.M.; Balzer, A.; Jaeger, A.; Klug, G.
Bacteriochlorophyll-dependent expression of genes for pigment-binding proteins in Rhodobacter capsulatus involves the RegB/RegA two-component system
Mol. Genet. Genomics
267
202-209
2002
Rhodobacter capsulatus (D5AP79), Rhodobacter capsulatus SB1003 (D5AP79)
brenda
Teramura, M.; Tsukatani, Y.; Harada, J.; Hirose, M.; Tamiaki, H.
Stereoselective C3-substituent modification and substrate channeling by oxidoreductase BchC in bacteriochlorophyll a biosynthesis
FEBS Lett.
593
799-809
2019
Chlorobaculum tepidum, Chlorobaculum tepidum (Q93ST5), Rhodobacter capsulatus
brenda
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