Primary structure of soybean lipoxygenase-1.

Shibata, Daisuke; Steczko, Janusz; Dixon, Jack E.; Hermodson, Mark A.; Yazdanparast, Razieh; Axelrod, Bernard

doi:10.1016/s0021-9258(18)61079-8

Cited by 163 publications

(28 citation statements)

References 38 publications

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“…The three major isozymes of soybean seed, lipoxygenase L-l (Shibata et al, 1987), lipoxygenase L-2 (Shibata et al, 1988), and lipoxygenase L-3 (Yenofsky et al, 1988), were the first lipoxygenases to be sequenced. We noted a strongly conserved motif of 38 amino acid residues which included 5 conserved histidines and suggested this region as a putative iron binding site (Shibata et al, 1988).…”

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confidence: 99%

Crystallographic determination of the active site iron and its ligands in soybean lipoxygenase L-1

Minor¹,

Steczko²,

Bolin³

et al. 1993

Biochemistry

159

100

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Five ligands of the active site iron atom in soybean lipoxygenase L-1 have been identified from the electron density map of the crystallized enzyme. The position of the iron atom can be readily and independently located from an anomalous difference electron density map. The ligands identified are His-499, His-504, His-690, Asn-694, and Ile-839, the carboxy-terminal residue. Our previous view that these three histidines are essential for activity and binding of iron, based on site-specific mutation studies, is confirmed. A sixth protein ligand is not present, and the sixth coordination site opens into a wide cleft. The structure of the soybean lipoxygenase was solved by multiple anomalous isomorphous replacements.

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confidence: 99%

Crystallographic determination of the active site iron and its ligands in soybean lipoxygenase L-1

Minor¹,

Steczko²,

Bolin³

et al. 1993

Biochemistry

159

100

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“…The enzyme is a single polypeptide of molecular weight 94 000 and when expressed in kidney 293 cells (Wu et al, 1991a) it retains the ability to carboxylate the FLEEL pentapeptide. The C-terminal portion of carboxylase shares approximately 19% sequence homology over a stretch of 198 amino acids with a well-studied dioxygenase, soybean lipoxygenase 1 (Vliegenthart & Veldink, 1982;Shibata et al, 1987). The soybean lipoxygenase is one of four isozymes that are part of a large family of lipoxygenases from plants and animals that share 40-90% sequence homologies in the C-terminal regions.…”

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confidence: 99%

Dioxygen transfer during vitamin K dependent carboxylase catalysis

Kuliopulos¹,

Hubbard²,

Lam³

et al. 1992

Biochemistry

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The vitamin K dependent carboxylase of liver microsomes is involved in the posttranslational modification of certain serine protease zymogens which are critical components of the blood clotting cascade. During coupled carboxylation/oxygenation this carboxylase converts glutamate residues, dihydrovitamin K, CO2, and O2 to a gamma-carboxyglutamyl (Gla) residue, vitamin K (2R,3S)-epoxide, and H2O with a stoichiometry of 1:1 for all substrates and products. In this paper we investigate the role of molecular oxygen in the reaction by following the course of the oxygen atoms using 18O2. Two different mass spectroscopic techniques, electron ionization positive ion mass spectrometry and supercritical fluid chromatography-negative ion chemical ionization mass spectrometry, were used to quantitate the amount of 18O incorporation into the various oxygens of the vitamin K epoxide product. We found that 0.95 mol atoms of oxygen were incorporated into the epoxide oxygen, 0.05 mol atoms of oxygen were incorporated into the quinone oxygen of vitamin K epoxide, and the remaining ca. 1.0 mol atoms of oxygen were incorporated into H2O. No incorporation of oxygen into vitamin K epoxide from 50% H2(18)O was observed. Thus, the carboxylase operates as a dioxygenase 5% of the time during carboxylation/oxygenation. The relevance of these findings with respect to the nonenzymic "basicity enhancement" model proposed by Ham and Dowd [(1990) J. Am. Chem. Soc. 112, 1660-1661] is discussed.

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“…Because oxidation commonly occurs regiospecifically, with oxygen incorporated at either C9 or C13 (Gardner, 1991;Robinson et al, 1995), LOXs can also be classified as 9-or 13-LOXs. For example, soy LOX-1 is a 13-LOX, LOX-2 is a 9-/13-LOX, and soy LOX-3 is a 9-LOX or 9/13-LOX (Baysal & Demirdöven, 2007;Robinson et al, 1995;Shibata, 1987Shibata, , 1988. Furthermore, soy LOX-1 prefers free fatty acids as substrates, as do most type I LOXs, whereas LOX-2 and -3 also oxygenate esterified fatty acids, as do most type II LOXs (Baysal & Demirdöven, 2007;Eskin et al, 1977;Zhang et al, 2020).…”

Section: Enzyme-catalyzed Oxidation Reactions That Produce Off-flavor...mentioning

confidence: 99%

Flavor challenges in extruded plant‐based meat alternatives: A review

Wang

Tuccillo

Lampi

et al. 2022

Comp Rev Food Sci Food Safe

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Demand for plant-based meat alternatives has increased in recent years due to concerns about health, ethics, the environment, and animal welfare. Nevertheless, the market share of plant-based meat alternatives must increase significantly if they are to support sustainable food production and consumption. Flavor is an important limiting factor of the acceptability and marketability of plant-based meat alternatives. Undesirable chemosensory perceptions, such as a beany flavor, bitter taste, and astringency, are often associated with plant proteins and products that use them. This study reviewed 276 articles to answer the following five research questions: (1) What are the volatile and nonvolatile compounds responsible for off-flavors? (2) What are the mechanisms by which these flavor compounds are generated? (3) What is the influence of thermal extrusion cooking (the primary structuring technique to transform plant proteins into fibrous products that resemble meat in texture) on the flavor characteristics of plant proteins? (4) What techniques are used in measuring the flavor properties of plant-based proteins and products? (5) What strategies can be used to reduce off-flavors and improve the sensory appeal of plant-based meat alternatives? This article comprehensively discusses, for the first time, the flavor issues of plant-based meat alternatives and the technologies available to improve flavor and, ultimately, acceptability.

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Primary structure of soybean lipoxygenase-1.

Cited by 163 publications

References 38 publications

Crystallographic determination of the active site iron and its ligands in soybean lipoxygenase L-1

Crystallographic determination of the active site iron and its ligands in soybean lipoxygenase L-1

Dioxygen transfer during vitamin K dependent carboxylase catalysis

Flavor challenges in extruded plant‐based meat alternatives: A review

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