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Biomedical subjects

S Y Choi

Publications and source records attributed to S Y Choi.

At least 127 records · Page 7Linked to original sources
PubMed1995

The Moloney leukemia retroviral long terminal repeat trans-activates AP-1-inducible genes and AP-1 transcription factor binding.

Moloney murine leukemia virus (Mo-MuLV) is a thymotropic and leukemogenic retrovirus which causes T lymphomas. The long terminal repeat (LTR) of Mo-MuLV affects the regulation of a number of cellular genes, including collagenase IV, monocyte chemoattractant protein-1, and c-jun genes, all of which contain 12-O-tetradecanoylphorbol-13-acetate-responsive element consensus sites within their promoters. We report here that Mo-MuLV stimulates the collagenase IV gene through transcription factor AP-1, and that the expression of a subgenomic portion of Mo-MuLV LTR alone is sufficient for this effect. Transient or stable expression of the viral LTR increases cellular AP-1 DNA binding activity. The collagenase IV 12-O-tetradecanoylphorbol-13-acetate-responsive element consensus sequence was shown to be required for this trans-activation. Deletions or mutations of this consensus site which abolished AP-1 binding also abolished trans-activation by the LTR. Transient or stable transfection of the viral LTR into cells stimulated c-jun gene expression, suggesting one mechanism whereby the viral LTR may induce cellular AP-1 activity. Thus, the Mo-MuLV LTR, through activation of the transcription factor AP-1, is capable of regulating cellular gene expression, including the induction of proto-oncogenes. This activity may be relevant to the mechanisms whereby retroviruses which do not contain oncogenes induce neoplasia.

3T3 Cells↗
PubMed1995

Lipoprotein lipase association with lipoproteins involves protein-protein interaction with apolipoprotein B.

Lipoprotein lipase (LPL) hydrolyzes chylomicron and very low density lipoprotein (VLDL) triglycerides and potentiates the cellular uptake of lipoproteins. These LPL-lipoprotein associations could involve only protein-lipid interaction, or they could be modulated by apolipoproteins (apo). ApoB is the major protein component of chylomicrons, VLDL, and low density lipoprotein (LDL). ApoB100, a large glycoprotein with a molecular mass of 550 kDa, is composed of several functional domains. A carboxyl-terminal region of the protein is the ligand for the LDL receptor. There are several hydrophobic domains that are believed to be important in lipid binding. The relatively hydrophilic amino-terminal region of apoB, however, has no known function. Using solid phase assays we quantified LPL-lipoprotein complex formation. On a molar basis, severalfold greater amounts of LPL bound to LDL and VLDL than to high density lipoprotein at all the concentrations of LPL tested (0.9-55 nM). To assess the roles of LDL protein versus lipid, we performed competition and ligand blotting experiments. LDL and an amino-terminal fragment of apoB competed better for 125I-LPL binding to LDL than did lipid emulsion particles. Delipidation of LDL-coated plates did not alter LPL binding. On ligand blots, LPL bound to amino-terminal fragments of apoB generated by thrombin digestion but not to apoA1, apoE, or carboxyl-terminal fragments of apoB. Further evidence for LPL interaction with the amino-terminal region of apoB was obtained using anti-apoB monoclonal antibodies. Antibodies directed against the amino-terminal regions of apoB blocked LPL interaction with LDL, whereas those against the carboxyl-terminal region of apoB did not inhibit LPL interaction with LDL. Thus, we conclude that a specific interaction between LPL and the amino-terminal region of apoB may facilitate LPL association with circulating lipoproteins.

Antibodies, Monoclonal↗
PubMed1995

Photoaffinity labeling of retinoic acid-binding proteins.

Retinoid-binding proteins are essential mediators of vitamin A function in vertebrate organisms. They solubilize and stabilize retinoids, and they direct the intercellular and intracellular trafficking, transport, and metabolic function of vitamin A compounds in vision and in growth and development. Although many soluble retinoid-binding proteins and receptors have been purified and extensively characterized, relatively few membrane-associated enzymes and other proteins that interact with retinoids have been isolated and studied, due primarily to their inherent instabilities during purification. In an effort to identify and purify previously uncharacterized retinoid-binding proteins, it is shown that radioactively labeled all-trans-retinoic acid can be used as a photoaffinity labeling reagent to specifically tag two known retinoic acid-binding proteins, cellular retinoic acid-binding protein and albumin, in complex mixtures of cytosolic proteins. Additionally, a number of other soluble and membrane-associated proteins that bind all-trans-[11,12-3H]retinoic acid with high specificity are labeled utilizing the same photoaffinity techniques. Most of these labeled proteins have molecular weights that do not correspond to any known retinoid-binding proteins. Thus, photoaffinity labeling with all-trans-retinoic acid and related photoactivatable retinoids is a method that should prove extremely useful in the identification and purification of novel soluble and membrane-associated retinoid-binding proteins from ocular and nonocular tissues.

Affinity Labels↗
PubMed1995

Ginsenosides activate DNA polymerase delta from bovine placenta.

The activation of a DNA polymerase delta (pol delta) purified from bovine placenta by ginsenosides from Panax Ginseng C. A. Meyer has been studied. Preincubation of the enzyme with ginsenosides increased the polymerase activity 2.2-fold in a dose-dependent manner. There was a reproducible decrease in Km, in addition to a substantial increase in Vmax, in response to increasing concentrations of ginsenosides. Ginsenosides also activated the proofreading ability of 3'- to 5'-exonuclease activity associated with DNA pol delta. The coordinated activation of both polymerase and exonuclease activities of DNA pol delta by ginsenosides is consistent with the view that its polymerase and its exonuclease activities residue on the same protein molecule. UV/Vis difference spectroscopic studies suggested that the activation of DNA pol delta by ginsenosides might be due to the conformational change induced by ginsenosides binding.

Animals↗
PubMed1995

Production and characterization of monoclonal antibodies to bovine brain succinic semialdehyde reductase.

Monoclonal antibodies against bovine brain succinic semialdehyde reductase were produced and characterized. A total of nine monoclonal antibodies recognizing different epitopes of the enzyme were obtained, of which two inhibited the enzyme activity and three stained cytosol of rat spinal cord neurons as observed by indirect immunofluorescence microscopy. When unfractionated total proteins of bovine brain homogenate were separated by gel electrophoresis and immunoblotted, the antibodies specifically recognized a single protein band of 34 kDa, which comigrates with purified bovine succinic semialdehyde reductase. Using the antisuccinic semialdehyde reductase antibodies as probes, we investigated the cross-reactivities of brain succinic semialdehyde reductases from some mammalian and an avian species. The immunoreactive bands on western blots appeared to be the same in molecular mass--34 kDa--in all animal species tested, including humans. The result indicates that brain succinic semialdehyde reductase is distinct from other aldehyde reductases and that mammalian brains contain only one succinic semialdehyde reductase. Moreover, the enzymes among the species are immunologically very similar, although some properties of the enzymes reported previously were different from one another.

Animals↗
PubMed1995

A transcript from the long terminal repeats of a murine retrovirus associated with trans activation of cellular genes.

Infection of human or murine cells with murine leukemia viruses rapidly increases the expression of a number of genes that belong to the immunoglobulin superfamily and are involved in T-lymphocyte activation, including the class I major histocompatibility complex antigens. We have reported recently that the long terminal repeat (LTR) of Moloney murine leukemia virus encodes a trans activator which induces transcription and expression of class I major histocompatibility complex genes and certain cytokine genes. The portion of the LTR responsible for trans activation was mapped by deletions to lie within the U3 region. We demonstrate here that a transcript is initiated within the U3 region and that its presence correlates with the trans-activating activity. Analysis of the LTR region reveals a potential internal promoter element for RNA polymerase III transcription within the U3 region. Studies with polymerase inhibitors suggest that this LTR transcript, designated let (LTR-encoded trans activator), is a product of RNA polymerase III. The mechanisms whereby RNA leukemia viruses cause lymphoid neoplasia after a long latent period have been extensively studied but are only partially understood. The region of the LTR identified here as being important in trans activation has recently been shown to be a critical determinant of the leukemogenicity and latency of Moloney murine leukemia virus. These findings suggest a novel mechanism of retrovirus-induced activation of cellular gene expression, potentially contributing to leukemogenesis.

3T3 Cells↗
PubMed1995

Reliability and validity of the cognitive impairment diagnosing instrument (CIDI) in the elderly.

The reliability and validity of the Cognitive Impairment Diagnosing Instrument (CIDI) were studied in 67 nursing home elderly subjects and 251 elderly psychiatric patients. Its possible highest score is 77 and covers 10 subscales: short-term memory, long-term memory, concentration/calculation, abstract thinking, judgement, memory registration, higher cortical functions, orientation in time, orientation in place and object naming. Test-retest correlations were between 0.827 and 0.990 for the subscale scores and 0.984 for the total score. Inter-tester kappas for each item ranged from 0.200 to 1.000 with a mean of 0.698. Concordance rates were between 50.0 and 100.0% with a mean of 87.2%. Cronbach's alphas for the items of the individual subscales ranged from 0.702 to 0.915. Inter-subscale and subscale-total correlations ranged from 0.503 to 0.820 with a mean of 0.684 and from 0.721 to 0.883, respectively. Cronbach's alpha of the subscales was 0.934. Sensitivity and specificity were 93.3% and 93.8% at the cut-off point of 57.0/57.5 for dementia. Subscale and total scores were significantly different between the demented and non-demented. The total CIDI score was significantly correlated with scores of the Blessed Dementia Rating Scale and the Korean version of the Mini-Mental State Examination.

Aged↗
PubMed1995

Preventive effect of ginseng intake against various human cancers: a case-control study on 1987 pairs.

This study presents the risk of various cancers in relation to ginseng intake based on the data from a case-control study conducted in the Korea Cancer Center Hospital. Ginseng intakers had a decreased risk [odds ratio = 0.50, 95% confidence interval (CI) = 0.44-0.58] for cancer compared with nonintakers. On the type of ginseng, the odds ratios for cancer were 0.37 (95% CI = 0.29-0.46) for fresh ginseng extract intakers, 0.57 (95% CI = 0.48-0.68) for white ginseng extract intakers, 0.30 (95% CI = 0.22-0.41) for white ginseng powder intakers, and 0.20 (95% CI = 0.08-0.50) for red ginseng intakers. Intakers of fresh ginseng slice, fresh ginseng juice, and white ginseng tea, however, showed no decreasing risk. There was a decrease in risk with the rising frequency and duration of ginseng intake, showing a dose-response relationship. On the site of cancer, the odds ratios were 0.47 for cancer of the lip, oral cavity, and pharynx; 0.20 for esophageal cancer; 0.36 for stomach cancer; 0.42 for colorectal cancer; 0.48 for liver cancer; 0.22 for pancreatic cancer; 0.18 for laryngeal cancer; 0.55 for lung cancer; and 0.15 for ovarian cancer. In cancers of the female breast, uterine cervix, urinary bladder, and thyroid gland, however, there was no association with ginseng intake. In cancers of the lung, lip, oral cavity and pharynx, and liver, smokers with ginseng intake showed decreased odds ratios compared with smokers without ginseng intake. These findings support the view that ginseng intakers had a decreased risk for most cancers compared with nonintakers.(ABSTRACT TRUNCATED AT 250 WORDS)

Adolescent↗
PubMed1994

Bacterial glutamate racemase has high sequence similarity with myoglobins and forms an equimolar inactive complex with hemin.

Glutamate racemase (EC 5.1.1.3), an enzyme of microbial origin, shows significant sequence homology with mammalian myoglobins, in particular in the regions corresponding to the E and F helices, which constitute the heme binding pocket of myoglobins. Glutamate racemase binds tightly an equimolar amount of hemin, leading to loss of racemase activity. Although this enzyme shows homology with aspartate racemase, the latter does not bind hemin. The glutamate racemase gene of Pediococcus pentosaceus has a 795-nt open reading frame and encodes 265-amino acid residues, which form a monomeric protein (M(r) 29,000). Neither racemase has cofactors, but they contain essential cysteine residues [Yohda, M., Okada, H. & Kumagai, H. (1991) Biochim. Biophys. Acta 1089, 234-240].

Amino Acid Isomerases↗
PubMed1994

The long terminal repeats of a murine retrovirus encode a trans-activator for cellular genes.

Type C RNA leukemia viruses cause lymphoid neoplasia after an extended latent period by an unknown mechanism. Infection of human or murine cells with murine leukemia viruses rapidly increases the expression of genes belonging to the immunoglobulin superfamily and involved in T-lymphocyte activation, including the class I major histocompatibility complex antigens. We report here that the long terminal repeat (LTR) of Moloney murine leukemia virus encodes a novel trans-activator, which induces transcription and expression of class I major histocompatibility complex genes. The portion of the LTR responsible for trans-activation lies within the U3 region and can be excised from the LTR while maintaining its activity. Analysis of the U3 region of the LTR and its flanking sequences suggests that functional or regulatory elements for the trans-activity exist between nucleotides 32 and 219 of the LTR sequences. The region of the LTR identified here as important in trans-activation has been shown recently to be a critical determinant of leukemogenicity and latency of Moloney murine leukemia virus. These findings suggest a novel mechanism of retrovirus-induced activation of cellular gene expression, potentially contributing to leukemogenesis.

3T3 Cells↗
PubMed1994

An amino-terminal fragment of apolipoprotein B binds to lipoprotein lipase and may facilitate its binding to endothelial cells.

Lipoprotein lipase (LPL), the principal enzyme which hydrolyzes triglycerides in circulating plasma lipoproteins, functions while bound to the luminal surface of endothelial cells. LPL is a heparin-binding protein and has been assumed to associate with endothelial cell heparan sulfate proteoglycans (HSPG). Recently, using ligand blotting and affinity chromatography we identified a 116-kDa heparin-releasable LPL-binding protein (hrp-116) from endothelial cells which was not a HSPG (Sivaram, P., Klein, M. G., and Goldberg, I. J. (1992) J. Biol. Chem. 267, 16517-16522). This suggested that, like a number of other heparin-binding proteins, LPL binding to cells also involves non-HSPG proteins. Using heparin-agarose affinity chromatography, a 116-kDa LPL-binding protein was purified from endothelial cell extracts. Microsequencing of peptides generated by Lys-C protease digestion revealed complete homology with four different regions in the NH2-terminal part of human apolipoprotein B (apoB). Western blots using anti-apoB monoclonal antibodies (mAb) that recognize the NH2-terminal region of apoB confirmed that a 116-kDa fragment of apoB was present on endothelial cell membranes. Further evidence that LPL associates with the NH2-terminal region of apoB was obtained by showing 1) that an NH2-terminal fragment of apoB obtained from apoB-transfected CHO cells bound LPL on ligand blots and 2) that NH2-terminal fragments of apoB generated by thrombin digestion of low density lipoprotein bind LPL. Evidence that the NH2-terminal region of apoB mediates LPL interaction with endothelial cells was obtained using monoclonal antibodies. mAb3 and mAb19, which recognize epitopes near the NH2 terminus of apoB, inhibited 125I-LPL binding to cells by 60-65%. In contrast, mAb47, which has determinants at the COOH-terminal end of apoB, inhibited LPL binding by only about 10%. The inhibitory effects of mAb3 and mAb19 were abolished following treatment of cells with heparin, which removes the 116-kDa LPL-binding protein. Furthermore, incubation of 125I-LPL in medium containing an NH2-terminal apoB fragment reduced LPL binding to cells. These data suggest that an NH2-terminal fragment of apoB that binds to endothelial surfaces facilitates LPL binding to cells.

Amino Acid Sequence↗
PubMed1994

Fermentation and sensory characteristics of kimchi containing potassium chloride as a partial replacement for sodium chloride.

A study was designed to determine the effects of substituting up to 50% of the NaCl in kimchi, a fermented Chinese cabbage (Brassica pekinensis) product containing scallions, garlic, ginger and hot red pepper powder, with KCl. Brine water (15% salt) used to soak cabbage contained NaCl:KCl ratios of 1:0 (control), 5:1, 2:1 and 1:1 (wt:wt). Total acidity and pH of kimchi reached acceptable ranges of 0.4-0.6% (as lactic acid) and 4.4-4.7, respectively, after 13 days of incubation at 13 +/- 1 degree C. Kimchi made using brine water containing 5:1 and 2:1 (NaCl:KCl) salt ratios was characterized by faster growth of lactic acid bacteria and total aerobic microorganisms compared to the control formulation. Sensory qualities (saltiness, bitterness, sourness, hotness and texture) of kimchi prepared from cabbage soaked in brine containing NaCl and KCl at all test ratios were judged to be acceptable.

Bacteria↗
PubMed1994

Acceleration of uptake of LDL but not chylomicrons or chylomicron remnants by cells that secrete apoE and hepatic lipase.

ApoE is a ligand for the low density lipoprotein (LDL) receptor as well as for the LDL receptor-related protein (LRP). The enzyme hepatic lipase (HL) may also affect the uptake of lipoproteins by modifying their composition. We have tested the hypothesis that hepatic lipase and apoE can function as co-factors to alter the rate of lipoprotein uptake. Chinese hamster ovary (CHO) cells were transfected with cDNAs for rat hepatic lipase, human apoE or both HL and apoE. The secreted recombinant proteins were thoroughly characterized and had properties identical to the native proteins. Hepatic lipase and apoE were secreted at 0.17 and 1.25 micrograms/mg cell protein per hour, rates comparable to those in normal liver. 125I-labeled LDL, chylomicron remnants, or chylomicrons were added to media at concentrations near their Kd. In cells that secreted either apoE or hepatic lipase, or both apoE and hepatic lipase, LDL binding was significantly greater than with control cells (2.2-, 2-, 2-fold greater, respectively). Similar enhancement of LDL degradation was observed. In the presence of anti-LDL receptor antibodies, these values were reduced to control levels; thus, the enhanced uptake was mediated by the LDL receptor and not the LRP. The amount of LDL receptor protein, as judged by Western blotting, was similar in the various cell types. Incubation of control CHO cells with media from secreting transfected cells also increased the uptake of 125I-labeled LDL. Kinetic studies indicated that, in apoE-secreting cells, increased LDL binding is associated with a lower Kd and an unchanged Vmax as compared to the control cells; furthermore, when LDL were reisolated by column chromatography (but not by ultracentrifugation) from the incubations where apoE was being secreted, apoE was identified adherent to the LDL particles. Together, these results suggest that the effect is due to alteration of the lipoprotein and not the cell. In contrast, the uptake of 125I-labeled chylomicron remnants, and 125I-labeled chylomicrons was not greater in the transfected cells. Thus, in the amounts secreted by these cells, hepatic lipase and apoE do not convert chylomicrons to chylomicron remnants or alter the uptake of chylomicron remnants by either the LDL receptor or the LRP. The enhancement of LDL removal in cells that secrete hepatic lipase or apoE may help determine the amount of LDL removed by a particular tissue.

Animals↗
PubMed1993

Expression of glr (murI, dga) gene encoding glutamate racemase in Escherichia coli.

The murI (dga) gene of Escherichia coli is required for the biosynthesis of D-glutamate, an essential component of bacterial peptidoglycan (Doublet, P., van Heijetnoort, J., and Mengin-Lecreulx, D. (1992) J. Bacteriol. 174, 5772-5779; Dougherty, T. J., Thanassi, J. A., and Pucci, M. J. (1993) J. Bacteriol. 175, 111-116), but its gene product has not been identified. We found that the amino acid sequence of protein deduced from the nucleotide sequence of the open reading frame of murI gene (ORF1) shows a significant homology with that of glutamate racemase of Pediococcus pentosaceus. The amino acid sequence of glutamate racemase of Lactobacillus fermenti recently reported also shows a homology with the deduced amino acid sequence of ORFI (Gallo, K. A., and Knowles, J. R. (1993) Biochemistry 32, 3981-3990). The murI (dga) gene was ligated into a plasmid, pKK223-3, with a designed ribosome binding site and expressed in E. coli JM109 cells. Glutamate racemase was produced by the transformant cells, whereas the enzyme was not found in the host cells. Accordingly, we newly termed the gene glr, which is more relevant than murI and dga. We partially purified the enzyme to characterize it. The enzyme consists of two identical subunits with a molecular weight of about 31,000 in contrast to the P. pentosaceus enzyme, a monomer protein.

Amino Acid Isomerases↗
PubMed1993

A comparison of the roles of the low density lipoprotein (LDL) receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor in chylomicron remnant removal in the mouse in vivo.

Two cell surface molecules, the low density lipoprotein (LDL) receptor and the LDL receptor-related protein (LRP)/alpha 2-macroglobulin receptor, have been found to have a role in the removal of apoE-rich lipoproteins. To further study this process and to assess the relative contributions of these proteins to the removal of chylomicron remnants, we used an anti-LDL receptor antibody, activated alpha 2-macroglobulin and the 39-kDa receptor-associated protein (RAP) as inhibitors of chylomicron remnant removal in intact mice. The advantage of this study is that we were able to use the same litters of animals and batches of lipoprotein for the experiment. In cultured Chinese hamster ovary cells, the anti-LDL receptor antibody inhibited remnant uptake and degradation about 80% as well as did unlabeled remnants. It did not affect activated alpha 2-macroglobulin uptake or degradation. Activated alpha 2-macroglobulin did not inhibit remnant uptake in normal cells but is reported to block uptake in cells that lack LDL receptors. Chylomicron remnants blocked activated alpha 2-macroglobulin uptake as effectively as unlabeled activated alpha 2-macroglobulin. This confirmed that the two ligands are cross-competitors but suggests that the LDL receptor is the primary mediator of remnant uptake in cultured cells that express the LDL receptor. In vivo, pretreatment with the anti-LDL receptor antibody decreased remnant uptake 5 min after injection by one-third. The antibody did not affect the removal of activated alpha 2-macroglobulin. Activated alpha 2-macroglobulin had a small, but reproducible effect on remnant removal, decreasing it by about 7% at 5 min. Injection of chylomicron remnants affected activated alpha 2-macroglobulin removal slightly. A similar pattern, but somewhat greater effect was seen on the hepatic uptake of the ligands. Anti-LDL receptor antibody reduced chylomicron remnant uptake by about half, and activated alpha 2-macroglobulin reduced it by about 15%. Studies with RAP provided results generally similar to those with activated alpha 2-macroglobulin, although RAP appears to bind to a site not recognized by either remnants or activated alpha 2-macroglobulin in addition to sharing a site with these ligands. Together, these results add support for the hypothesis that, although both receptors can play a role in chylomicron remnant removal, in the normal mouse in vivo the LDL receptor plays a substantially greater role, making the role of the LRP difficult to appreciate. The same is true in cells that express LDL receptors.(ABSTRACT TRUNCATED AT 400 WORDS)

Animals↗
PubMed1993

Expression of a phosphorylation-resistant eukaryotic initiation factor 2 alpha-subunit mitigates heat shock inhibition of protein synthesis.

Protein synthesis is dramatically reduced upon exposure of cells to elevated temperature. Concordant with this inhibition, multiple phosphorylation and dephosphorylation reactions occur on specific eukaryotic initiation factors that are required for protein synthesis. Most notably, phosphorylation of the alpha-subunit of eukaryotic initiation factor-2 (eIF-2 alpha) on serine residue 51 occurs. To identify the importance of phosphorylation in control of protein synthesis, we have evaluated the effects of expression of a mutant eIF-2 alpha which is resistant to phosphorylation. Expression of a serine to alanine mutant at residue 51 of eIF-2 alpha partially protected cells from the inhibition of protein synthesis in response to heat treatment. The overexpressed serine to alanine 51 mutant subunit was incorporated into the eIF-2 heterotrimer and was resistant to phosphorylation. These results are consistent with the hypothesis that heat shock inhibition of translation is mediated in part through phosphorylation of eIF-2 alpha. Expression of the wild type or mutant eIF-2 alpha did not affect cell survival or induction of hsp70 mRNA upon heat shock, indicating that although eIF-2 alpha is a heat shock-induced protein, its increased synthesis during heat shock does not alter the heat-shock response.

Alanine↗
PubMed1993

Kinetics and mechanism of an NADPH-dependent succinic semialdehyde reductase from bovine brain.

An NADPH-dependent succinic semialdehyde reductase has been purified from bovine brain by several chromatographic procedures. The preparation appeared homogeneous on SDS/PAGE. The enzyme is a monomeric protein with a molecular mass of 28 kDa. A number of properties of the bovine brain enzyme, such as substrate specificity, specific activity, molecular mass, optimum pH, amino acid composition, and kinetic parameters, have been determined and compared with those reported for preparations from other sources. The results indicate that the enzyme isolated from bovine brain in the present study is different from those reported for preparations from other sources. The inhibition kinetic patterns obtained when the products of the reaction or substrate analogs are used as inhibitor of the reaction catalyzed by the enzyme are consistent with an ordered sequential mechanism involving the formation of an intermediate ternary complex and in which NADPH is the first substrate to bind the enzyme.

Amino Acids↗