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Information on EC 1.1.1.100 - 3-oxoacyl-[acyl-carrier-protein] reductase and Organism(s) Brassica napus and UniProt Accession Q949M3
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1.1.1.100 3-oxoacyl-[acyl-carrier-protein] reductaseIUBMB Comments
Exhibits a marked preference for acyl-carrier-protein derivatives over CoA derivatives as substrates.
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Word Map
- 1.1.1.100
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enoyl
- drug development
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transacylase
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3-oxoacyl-acyl-carrier-protein
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dehydrase
- enoyl-acp
-
3-oxoacyl-acyl
- acyl-acps
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beta-hydroxyacyl-acp
- fas-ii
- 4'-phosphopantetheine
- synthesis
The taxonomic range for the selected organisms is: Brassica napus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
beta-ketoacyl reductase, fabg1, beta-ketoacyl-acp reductase, fabg4, 3-oxoacyl-acp reductase, fabg3, beta-ketoacyl-acyl carrier protein reductase, 3-ketoacyl-acp reductase, fabg2, oar1p, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-ketoacyl acyl carrier protein reductase
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3-ketoacyl-acyl carrier protein reductase
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3-oxoacyl-[ACP]reductase
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beta-ketoacyl acyl carrier protein (ACP) reductase
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beta-ketoacyl reductase
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beta-ketoacyl thioester reductase
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beta-ketoacyl-ACP reductase
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beta-ketoacyl-acyl carrier protein reductase
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beta-ketoacyl-[acyl-carrier protein] (ACP) reductase
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NADPH-specific 3-oxoacyl-[acylcarrier protein]reductase
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reductase, 3-oxoacyl-[acyl carrier protein]
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ = a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+
belongs to family of short-chain alcohol dehydrogenases (SDR) with catalytic triad Ser154, Tyr167 and Lys171, catalytic mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
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-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
(3R)-3-hydroxyacyl-[acyl-carrier protein]:NADP+ oxidoreductase
Exhibits a marked preference for acyl-carrier-protein derivatives over CoA derivatives as substrates.
CAS REGISTRY NUMBER
COMMENTARY
37250-34-3
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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
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
acetoacetyl-CoA + NADPH + H+
D-beta-hydroxybutyryl-CoA + NADP+
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-
-
-
?
acetoacetyl-N-cysteamine + NADPH
D-3-hydroxybutyryl-N-cysteamine + NADP+
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-
-
-
?
acetoacetyl-[acyl-carrier protein] + NADPH
D-beta-hydroxybutyryl-[acyl-carrier protein] + NADP+
additional information
?
-
-
animals, yeast and Mycobacteria have fatty acid synthetase containing all the individual activities on one or two multifunctional polypeptide chains, plants and most bacterial systems, including E. coli, possess individual monofunctional enzymes and a separate acyl carrier protein
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-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
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-
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
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-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
belongs to family of short-chain alcohol dehydrogenases (SDR) with catalytic triade Ser154, Tyr167 and Lys171, catalytic mechanism
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
enzyme is part of the dissociable fatty acid synthase type II multienzyme complex for de novo synthesis of fatty acids from acetyl-CoA and malonyl-CoA
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-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
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first reduction step of fatty acid synthase
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-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
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enzyme in fatty acid synthesis
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-
?
acetoacetyl-[acyl-carrier protein] + NADPH
D-beta-hydroxybutyryl-[acyl-carrier protein] + NADP+
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-
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?
acetoacetyl-[acyl-carrier protein] + NADPH
D-beta-hydroxybutyryl-[acyl-carrier protein] + NADP+
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much greater specificity for acetoacetyl-ACP than for either of the model substrates acetoacetyl-CoA or acetoacetyl-N-acetylcysteamine
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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
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
enzyme is part of the dissociable fatty acid synthase type II multienzyme complex for de novo synthesis of fatty acids from acetyl-CoA and malonyl-CoA
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
first reduction step of fatty acid synthase
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
enzyme in fatty acid synthesis
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
136000
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purified enzyme, protein determination by calculation from absorption at 280 nm
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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). FABG3_BRANA
315
0
33140
Swiss-Prot
Chloroplast (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
animals, yeast and Mycobacteria have fatty acid synthetases containing all the individual activities on one or two multifunctional polypeptide chains, plants and most bacterial systems, including Escherichia coli, possess individual monofunctional enzymes and a separate acyl carrier protein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure determination and similarities within short-chain alcohol dehydrogenase family, catalytic mechanism
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
transformation with 3-oxoacyl-[acyl-carrier-protein] reductase in antisense orientation, driven by either the cauliflower mosaic virus 35S promoter or a seed-specific acyl carrier protein promoter. In plants with altered reductase activity, total seed yield is reduced in all cases. In less severely affected plant lines, seeds have a normal appearance and composition but the yield of seeds is reduced by approximately 50%. In more severely affected lines, reductions in both seed fatty acid content and the number of seeds produced per plant are evident, resulting in a 90% reduction in fatty acid synthesized per plant. Phenotypes are independent of the promoter used. In severely affected lines, a large proportion of seeds show precocious germination, and these have a reduced oleate content and increased levels of polyunsaturated 18-carbon fatty acids, compared with normal seeds of the same line
additional information
-
transformation with 3-oxoacyl-[acyl-carrier-protein] reductase in antisense orientation, driven by either the cauliflower mosaic virus 35S promoter or a seed-specific acyl carrier protein promoter. In plants with altered reductase activity, total seed yield is reduced in all cases. In less severely affected plant lines, seeds have a normal appearance and composition but the yield of seeds is reduced by approximately 50%. In more severely affected lines, reductions in both seed fatty acid content and the number of seeds produced per plant are evident, resulting in a 90% reduction in fatty acid synthesized per plant. Phenotypes are independent of the promoter used. In severely affected lines, a large proportion of seeds show precocious germination, and these have a reduced oleate content and increased levels of polyunsaturated 18-carbon fatty acids, compared with normal seeds of the same line
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
transformation with 3-oxoacyl-[acyl-carrier-protein] reductase in antisense orientation, driven by either the cauliflower mosaic virus 35S promoter or a seed-specific acyl carrier protein promoter
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sheldon, P.S.; Safford, R.; Slabas, A.R.; Kekwick, R.G.O.
3-Oxoacyl-[acyl carrier protein] reductase: a component of plant fatty acid synthase
Biochem. Soc. Trans.
16
392-393
1988
Persea americana, Brassica napus
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Sheldon, P.S.; Kekwick, R.G.O.; Smith, C.G.; Sidebottom, C.; Slabas, A.R.
3-Oxoacyl-[ACP] reductase from oil seed rape (Brassica napus)
Biochim. Biophys. Acta
1130
151-159
1992
Brassica napus
Fisher, M.; Sedelnikowa, S.E.; Martindale, W.; Thomas, N.C.; Simon, J.W.; Slabas, A.R.; Rafferty, J.B.
Crystallization of the NADP-dependent beta-keto acyl-carrier protein reductase from Brassica napus
Acta Crystallogr. Sect. D
56
86-88
2000
Brassica napus
Fisher, M.; Kroon, J.T.M.; Martindale, W.; Stuitje, A.R.; Slabas, A.R.; Rafferty, J.B.
The x-ray structure of Brassica napus beta-keto acyl carrier protein reductase and its implications for substrate binding and catalysis
Structure
8
339-347
2000
Brassica napus, Escherichia coli
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