rat hepatic microsomal trans-2-enoyl-CoA reductases with cofactor requirement (NADH or NADPH) depending on chain length of substrates are characterized. Since no cis-2-enoyl-CoA compounds are tested as substrates a classification according to EC 1.3.1.8, EC 1.3.1.38 or EC 1.3.1.44 is impossible
BatG encodes a functional FabI isozyme which confers full resistance to kalimantacin/batumin and complements FabI. BatG is, similarity to trans-2-enoyl-ACP reductases, involved in the formation of a saturated acyl-ACP by an NAD(P)H-dependent reduction of the trans-2-enoyl-ACP double bond, which is essential for the final step of the elongation cycle of fatty acid biosynthesis. BatG knockout does not influence the kalimantacin/batumin, kal/bat, biosynthesis structurally. Kalimantacin/batumin biosynthesis is BatG-independent, despite BatG localization in the operon among kal/bat tailoring enzymes, overview
BatG encodes a functional FabI isozyme which confers full resistance to kalimantacin/batumin and complements FabI. BatG is, similarity to trans-2-enoyl-ACP reductases, involved in the formation of a saturated acyl-ACP by an NAD(P)H-dependent reduction of the trans-2-enoyl-ACP double bond, which is essential for the final step of the elongation cycle of fatty acid biosynthesis. BatG knockout does not influence the kalimantacin/batumin, kal/bat, biosynthesis structurally. Kalimantacin/batumin biosynthesis is BatG-independent, despite BatG localization in the operon among kal/bat tailoring enzymes, overview
rat hepatic microsomal long-chain and short-chain trans-2-enoyl-CoA reductases with cofactor requirement (NADH or NADPH) depending on substrate chain length are characterized. Since no cis-2-enoyl-CoA compounds are tested as substrates a classification according to EC 1.3.1.8, EC 1.3.1.38 or EC 1.3.1.44 is impossible
rat hepatic microsomal trans-2-enoyl-CoA reductases with cofactor requirement (NADH or NADPH) depending on chain length of substrates are characterized. Since no cis-2-enoyl-CoA substances are tested as substrates a classification according to EC 1.3.1.8, EC 1.3.1.38 or EC 1.3.1.44 is impossible
mutant Y240F, pH not specified in the publication, temperature not specified in the publication; pH and temperature not specified in the publication, mutant Y240F
mutant L276A/V277A, pH not specified in the publication, temperature not specified in the publication; pH and temperature not specified in the publication, mutant L276A/V277A
pH and temperature not specified in the publication, wild-type; wild-type, pH not specified in the publication, temperature not specified in the publication
mutant F295A, pH not specified in the publication, temperature not specified in the publication; pH and temperature not specified in the publication, mutant F295A
mutant L291A, pH not specified in the publication, temperature not specified in the publication; pH and temperature not specified in the publication, mutant L291A
mutant Y370A, pH not specified in the publication, temperature not specified in the publication; pH and temperature not specified in the publication, mutant Y370A
mutant I287A, pH not specified in the publication, temperature not specified in the publication; pH and temperature not specified in the publication, mutant I287A
mutant L276A/V277A/F295A, pH not specified in the publication, temperature not specified in the publication; pH and temperature not specified in the publication, mutant L276A/V277A/F295A
mutant Y240F, pH not specified in the publication, temperature not specified in the publication; pH and temperature not specified in the publication, mutant Y240F
mutant I287A, pH not specified in the publication, temperature not specified in the publication; pH and temperature not specified in the publication, mutant I287A
mutant L276A/V277A, pH not specified in the publication, temperature not specified in the publication; pH and temperature not specified in the publication, mutant L276A/V277A
mutant L276A/V277A/F295A, pH not specified in the publication, temperature not specified in the publication; pH and temperature not specified in the publication, mutant L276A/V277A/F295A
mutant L291A, pH not specified in the publication, temperature not specified in the publication; pH and temperature not specified in the publication, mutant L291A
mutant F295A, pH not specified in the publication, temperature not specified in the publication; pH and temperature not specified in the publication, mutant F295A
pH and temperature not specified in the publication, wild-type; wild-type, pH not specified in the publication, temperature not specified in the publication
mutant Y370A, pH not specified in the publication, temperature not specified in the publication; pH and temperature not specified in the publication, mutant Y370A
mutant Y240F, pH not specified in the publication, temperature not specified in the publication; pH and temperature not specified in the publication, mutant Y240F
mutant I287A, pH not specified in the publication, temperature not specified in the publication; pH and temperature not specified in the publication, mutant I287A
mutant L276A/V277A/F295A, pH not specified in the publication, temperature not specified in the publication; pH and temperature not specified in the publication, mutant L276A/V277A/F295A
mutant L276A/V277A, pH not specified in the publication, temperature not specified in the publication; pH and temperature not specified in the publication, mutant L276A/V277A
mutant L291A, pH not specified in the publication, temperature not specified in the publication; pH and temperature not specified in the publication, mutant L291A
mutant Y370A, pH not specified in the publication, temperature not specified in the publication; pH and temperature not specified in the publication, mutant Y370A
mutant F295A, pH not specified in the publication, temperature not specified in the publication; pH and temperature not specified in the publication, mutant F295A
pH and temperature not specified in the publication, wild-type; wild-type, pH not specified in the publication, temperature not specified in the publication
pH and temperature not specified in the publication, 0.5 mM inhibitor, wild-type; wild-type, pH not specified in the publication, temperature not specified in the publication
pH and temperature not specified in the publication, 0.05 mM inhibitor, wild-type; wild-type, pH not specified in the publication, temperature not specified in the publication
mutant I287A, pH not specified in the publication, temperature not specified in the publication; pH and temperature not specified in the publication, 0.00025 mM inhibitor, mutant I287A
pH and temperature not specified in the publication, 0.001 mM inhibitor, wild-type; wild-type, pH not specified in the publication, temperature not specified in the publication
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with NAD+, vapor diffusion method; structures of CaTER in apo form at 2.1 A resolution, in complex with NADH at 2.0 A resolution and in complex with NAD+ at 2.7 A resolution
purified and crystallized as an apoenzyme and in a complex form with NADH and triclosan. The crystals of native and complexed FabI diffract to resolutions of 2.6 and 1.8 A, respectively. The crystals both belong to space group P2-1, with unit-cell parameters a = 117.32, b = 155.844, c = 129.448 A , beta = 111.061° for the native enzyme and a = 64.784, b = 107.573, c = 73.517 A, beta = 116.162° for the complex
phage library screening, DNA and amino acid sequence determination and analysis, phylogenetic analysis, functional expression as His-tagged enzyme in Escherichia coli
wild-type and deletion mutant BatG expression in Pseudomonas fluorescens strain BCCM_ID9359, Escherichia coli, and Staphylococcus aureus, confers resistance against kalimantacin/batumin
kcat slightly decreased compared to wild-type, Km (NADH) decreased compared to wild-type; the mutant shows 198% activity compared to the wild type enzyme
kcat slightly decreased compared to wild-type, Km (NADH) increased compared to wild-type; the mutant shows 67 activity compared to the wild type enzyme
site-directed mutagenesis, mutation of putative catalytic residue, mutant can only be stably expressed in Escherichia coli strain BL21(DE3) if altered to a soluble enzyme form dependent on IPTG induction
mutant shows significant decreased kcat values compared to wild-type, mutant exhibit larger increases in catalytic efficiency on the longer hexanoyl-CoA substrate (versus the crotonyl-CoA substrate) of 100 and 17fold compared to that of the wild type (7fold) suggesting suggest these mutations may increase the accessibility of the longer acyl chain to the active site pocket. Mutant shows a much lower Ki (lauroyl-CoA) than wild-type
mutant shows significant decreased kcat values compared to wild-type, mutant exhibit larger increases in catalytic efficiency on the longer hexanoyl-CoA substrate (versus the crotonyl-CoA substrate) of 100 and 17fold compared to that of the wild type (7fold) suggesting suggest these mutations may increase the accessibility of the longer acyl chain to the active site pocket
mutant shows significant decreased kcat values compared to wild-type, mutant exhibit larger increases in catalytic efficiency on the longer hexanoyl-CoA substrate (versus the crotonyl-CoA substrate) of 100 and 17fold compared to that of the wild type (7fold) suggesting suggest these mutations may increase the accessibility of the longer acyl chain to the active site pocket. Mutant shows a much lower Ki (lauroyl-CoA) than wild-type
construction of stable mutants for optimization of expression of enzyme in Escherichia coli, absolutely dependent on IPTG, phenotype alterations, overview
Kinetic evidence for two separate trans-2-enoyl CoA reductases in rat hepatic microsomes: NADPH-specific short chain- and NAD(P)H-dependent long chain-reductase
Involvement of one of two enoyl-CoA hydratases and enoyl-CoA reductase in the acetyl-CoA-dependent elongation of medium chain fatty acids by Mycobacterium smegmatis
Poletto, S.S.; da Fonseca, I.O.; de Carvalho, L.P.; Basso, L.A.; Santos, D.S.
Selection of an Escherichia coli host that expresses mutant forms of Mycobacterium tuberculosis 2-trans enoyl-ACP(CoA) reductase and 3-ketoacyl-ACP(CoA) reductase enzymes
Hu, K.; Zhao, M.; Zhang, T.; Zha, M.; Zhong, C.; Jiang, Y.; Ding, J.
Structures of trans-2-enoyl-CoA reductases from Clostridium acetobutylicum and Treponema denticola: insights into the substrate specificity and the catalytic mechanism
Increasing n-butanol production with Saccharomyces cerevisiae by optimizing acetyl-CoA synthesis, NADH levels and trans-2-enoyl-CoA reductase expression