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Chemical modification of an essential lysine at the active site of enoyl-CoA reductase in fatty acid synthetase

Archives of biochemistry and biophysics, 1980-04, Vol.201 (1), p.313-321

1980

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Presence of one essential arginine that specifically binds the 2′-phosphate of NADPH on each of the ketoacyl reductase and enoyl reductase active sites of fatty acid synthetase

Archives of biochemistry and biophysics, 1980-02, Vol.199 (2), p.457-464

1980

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Developmental pattern of the expression of malonyl-CoA decarboxylase gene and the production of unique lipids in the goose uropygial glands

Archives of biochemistry and biophysics, 1987-08, Vol.256 (2), p.446-454

1987

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[13] Fatty acid synthase from the uropygial gland of goose

Methods in Enzymology, 1981, Vol.71, p.103-109

1981

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[18] Structure and function of engineered Pseudomonas mendocina lipase

Methods in Enzymology, 1997, Vol.284, p.298-317

1997

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Purification and properties of malonyl-coenzyme A decarboxylase, a regulatory enzyme from the uropygial gland of goose

Archives of biochemistry and biophysics, 1976-01, Vol.177 (2), p.539-551

1976

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Biosynthesis of aromatic monoterpenes: Conversion of γ-terpinene to p-cymene and thymol in Thymus vulgaris L

Archives of biochemistry and biophysics, 1978-04, Vol.187 (2), p.307-314

1978

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Cloning and sequencing of the cDNA for S-acyl fatty acid synthase thioesterase from the uropygial gland of mallard duck

The Journal of biological chemistry, 1985-12, Vol.260 (29), p.15953-15958

1985

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γ-Terpinene synthetase: A key enzyme in the biosynthesis of aromatic monoterpenes

Archives of biochemistry and biophysics, 1978-11, Vol.191 (1), p.400-411

1978

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Biosynthesis of aromatic monoterpenes

Archives of biochemistry and biophysics, 1978-04, Vol.187 (2), p.307-314

1978

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Sequence of a tryptic peptide from the NADPH binding site of the enoyl reductase domain of fatty acid synthase

Archives of biochemistry and biophysics, 1983-02, Vol.220 (2), p.652-656

1983

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Determination of structure and composition of suberin from the roots of carrot, parsnip, rutabaga, turnip, red beet, and sweet potato by combined gas-liquid chromatography and mass spectrometry

Plant physiology (Bethesda), 1975-03, Vol.55 (3), p.567-573

1975

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Specific modification of the condensation domain of fatty acid synthase and the determination of the primary structure of the modified active site peptides

Archives of biochemistry and biophysics, 1984-01, Vol.230 (1), p.117-128

1984

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Structure-activity relationships of protease and lipase variants generated by protein engineering

Enzyme and microbial technology, 1991-06, Vol.13 (6), p.524-524

1991

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Role of the enoyl reductase domain in the regulation of fatty acid synthase activity by interdomain interaction

The Journal of biological chemistry, 1981-08, Vol.256 (16), p.8379-8383

1981

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Determination of structure and composition of suberin from the roots of carrot, parsnip, rutabaga, turnip, red beet, and sweetpotato by combined gas-liquid chromatography and mass spectrometry

Plant physiology (Bethesda), 1975, Vol.55

1975

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[20] Malonyl-CoA decarboxylase from avian, mammalian, and microbial sources: EC 4.1.1.9 Malonyl-CoA carboxy-lyase

Methods in Enzymology, 1981, Vol.71, p.150-163

1981

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New fluorescence evidence that each peptide of fatty acid synthetase has a keto and an enoyl reductase domain with different affinities for NADPH

The Journal of biological chemistry, 1980-12, Vol.255 (23), p.11313-11319

1980

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Evidence that the coenzyme a requirement for avian fatty acid synthase is not for the ermination reaction

International journal of biochemistry, 1982, Vol.14 (6), p.445-448

1982

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Evidence that the coenzyme A requirement for avian fatty acid synthase is not for the termination reaction

International journal of biochemistry, 1982, Vol.14 (6), p.445-448

1982

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Enzymatic reduction of phenylglyoxal and 2,3-butanedione, two commonly used arginine-modifying reagents, by the ketoacyl reductase domain of fatty acid synthase

International journal of biochemistry, 1986, Vol.18 (9), p.807-812

1986

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Selective chemical modification of the active sites of the ketoacyl reductase and enoyl reductase of fatty acid synthetase from lactating rat mammary glands

International journal of biochemistry, 1980, Vol.12 (4), p.591-596

1980

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Primary structure of a chymotryptic peptide containing the “active serine” of the thioesterase domain of fatty acid synthase

Biochemical and biophysical research communications, 1981-11, Vol.103 (2), p.377-382

1981

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Chemical modification of an essential lysine at the active site of enoyl-CoA reductase in fatty acid synthetase

Presence of one essential arginine that specifically binds the 2′-phosphate of NADPH on each of the ketoacyl reductase and enoyl reductase active sites of fatty acid synthetase

Developmental pattern of the expression of malonyl-CoA decarboxylase gene and the production of unique lipids in the goose uropygial glands

[13] Fatty acid synthase from the uropygial gland of goose

[18] Structure and function of engineered Pseudomonas mendocina lipase

Purification and properties of malonyl-coenzyme A decarboxylase, a regulatory enzyme from the uropygial gland of goose

Biosynthesis of aromatic monoterpenes: Conversion of γ-terpinene to p-cymene and thymol in Thymus vulgaris L

Cloning and sequencing of the cDNA for S-acyl fatty acid synthase thioesterase from the uropygial gland of mallard duck

γ-Terpinene synthetase: A key enzyme in the biosynthesis of aromatic monoterpenes

Biosynthesis of aromatic monoterpenes

Sequence of a tryptic peptide from the NADPH binding site of the enoyl reductase domain of fatty acid synthase

Determination of structure and composition of suberin from the roots of carrot, parsnip, rutabaga, turnip, red beet, and sweet potato by combined gas-liquid chromatography and mass spectrometry

Specific modification of the condensation domain of fatty acid synthase and the determination of the primary structure of the modified active site peptides

Structure-activity relationships of protease and lipase variants generated by protein engineering

Role of the enoyl reductase domain in the regulation of fatty acid synthase activity by interdomain interaction

Determination of structure and composition of suberin from the roots of carrot, parsnip, rutabaga, turnip, red beet, and sweetpotato by combined gas-liquid chromatography and mass spectrometry

[20] Malonyl-CoA decarboxylase from avian, mammalian, and microbial sources: EC 4.1.1.9 Malonyl-CoA carboxy-lyase

New fluorescence evidence that each peptide of fatty acid synthetase has a keto and an enoyl reductase domain with different affinities for NADPH

Evidence that the coenzyme a requirement for avian fatty acid synthase is not for the ermination reaction

Evidence that the coenzyme A requirement for avian fatty acid synthase is not for the termination reaction

Enzymatic reduction of phenylglyoxal and 2,3-butanedione, two commonly used arginine-modifying reagents, by the ketoacyl reductase domain of fatty acid synthase

Selective chemical modification of the active sites of the ketoacyl reductase and enoyl reductase of fatty acid synthetase from lactating rat mammary glands

Primary structure of a chymotryptic peptide containing the “active serine” of the thioesterase domain of fatty acid synthase

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