(Q27633168)

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Glutamate 170 of human l-3-hydroxyacyl-CoA dehydrogenase is required for proper orientation of the catalytic histidine and structural integrity of the enzyme

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Glutamate 170 of human l-3-hydroxyacyl-CoA dehydrogenase is required for proper orientation of the catalytic histidine and structural integrity of the enzyme (English)

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author name string

J J Barycki

1

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L K O'Brien

2

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A W Strauss

3

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L J Banaszak

4

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language of work or name

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publication date

28 September 2001

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Journal of Biological Chemistry

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276

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39

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36718-26

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Histidine-450 is the catalytic residue of L-3-hydroxyacyl coenzyme A dehydrogenase associated with the large alpha-subunit of the multienzyme complex of fatty acid oxidation from Escherichia coli.

1 reference

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Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary chain tracing at 2.8-A resolution

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The finer things in X-ray diffraction data collection

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Pfam 3.1: 1313 multiple alignments and profile HMMs match the majority of proteins

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The large subunit of the pig heart mitochondrial membrane-bound beta-oxidation complex is a long-chain enoyl-CoA hydratase: 3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme.

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Inherited long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency and a fetal-maternal interaction cause maternal liver disease and other pregnancy complications

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Conserved supersecondary structural motif in NAD-dependent dehydrogenases

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Two mitochondrial 3-hydroxyacyl-CoA dehydrogenases in bovine liver

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D-2-Hydroxy-4-Methylvalerate Dehydrogenase from Lactobacillus Delbrueckii Subsp. Bulgaricus- II. Mutagenic analysis of catalytically important residues

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Spatial arrangement of coenzyme and substrates bound to L-3-hydroxyacyl-CoA dehydrogenase as studied by spin-labeled analogues of NAD+ and CoA

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10.1074/JBC.M104839200

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