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The first step in branched-chain amino acid biosynthesis is catalyzed by acetohydroxyacid synthase (EC 2.2.1.6). This reaction involves decarboxylation of pyruvate followed by condensation with either an additional pyruvate molecule or... more
AHAS I is an isozyme of acetohydroxyacid synthase which is apparently unique to enterobacteria. It has been known for over 20 years that it has many properties which are quite different from those of the other two enterobacterial AHASs... more
The increased prevalence of drug-resistant human pathogenic fungal diseases poses a major threat to global human health. Thus, new drugs are urgently required to combat these infections. Here, we demonstrate that acetohydroxyacid synthase... more
Recent studies have shown a relation between nutritional factors and prevalence of some chronic disease [1]. In response to increased concern regarding nutrition and health, the functional food markets have been developed. The functional... more
In silico analysis and molecular docking study of angiotensin I-converting enzyme inhibitory peptides from smooth-hound viscera protein hydrolysates fractionated by ultrafiltration, Food Chemistry (2017),
The use of herbicides represents an important risk to environmental health, thus their monitoring is of fundamental importance to prevent and control contamination. The development of nanobiosensors is a powerful alternative because of... more
Blood pressure is regulated by the renin angiotensin aldosterone system (RAAS). Renin-catalyzed conversion of angiotensinogen to angiotensin I is the rate-limiting step of the RAAS pathway, which arguably makes renin a better target for... more
Tuberculosis (TB) is one of the most dangerous infectious diseases and is caused by Mycobacterium bovis (Mb) and Mycobacterium tuberculosis (Mt). Branched-chain amino acid aminotransferases (BCATs) were reported to be the key enzyme for... more
In silico analysis and molecular docking study of angiotensin I-converting enzyme inhibitory peptides from smooth-hound viscera protein hydrolysates fractionated by ultrafiltration, Food Chemistry (2017),
Twelve compounds (100 M) had a predicted log P between −0.5 and −3.0 and inhibited AHAS activity by >40%. CE, IQ, and SMM showed dose-dependent inhibition of Bacillus anthracis AHAS (BAntx AHAS) with IC 50 values of 7.01 ± 0.81, 6.97 ±... more
The first step in the common pathway for the biosynthesis of branched chain amino acids is catalyzed by acetohydroxyacid synthase (AHAS). The AHAS is found in plants, fungi and bacteria. With an aim to identify new anti-tuberculosis drugs... more
In this study, the antihypertensive activity of Purafect®-smooth hound viscera protein hydrolysate (VPH) and its peptide fraction with molecular weight (MW) below 1 kDa (VPH-I) was investigated. In addition, the lipase inhibitory... more
The reaction between the intermediate 2-hydroxyethyl-thiamin diphosphate (HEThDP 2) and 2-ketobutyrate, in the third step of the catalytic cycle of acetodydroxy acid synthase, is addressed from a theoretical point of view by means of... more
A combined molecular modeling and molecular dynamics simulation was carried out to obtain an improved description of the yeast acetohydroxyacid synthase (AHAS) in aqueous solution. After a thorough homology modeling, the AHAS catalytic... more
Novel and innovative functional supplements and bioactive ingredients can be explored from the vast diversity of Malaysian natural based resources. These include freshwater fish and its byproducts, edible bird nest, marine seaweeds, and... more
Acetohydroxyacid synthase I (AHAS I), one of three isozymes in Escherichia coli catalyzing the first common step in the biosynthesis of branched amino acids, is composed of two kinds of subunits. The large catalytic (B) and small... more
Twelve compounds (100 M) had a predicted log P between −0.5 and −3.0 and inhibited AHAS activity by >40%. CE, IQ, and SMM showed dose-dependent inhibition of Bacillus anthracis AHAS (BAntx AHAS) with IC 50 values of 7.01 ± 0.81, 6.97 ±... more
This study attempts to investigate the activities of chymotrypsin-digested M. oleifera seed proteins and their peptide fractions on carbohydrate-hydrolyzing enzymes. Proteins from M. oleifera seeds were isolated using isoelectric point... more
AHAS I is an isozyme of acetohydroxyacid synthase which is apparently unique to enterobacteria. It has been known for over 20 years that it has many properties which are quite different from those of the other two enterobacterial AHASs... more
Five genes from the ilv-leu operon from Bacillus stearothermophilus have been sequenced. Acetohydroxyacid synthase (AHAS) and its subunits were separately cloned, purified, and characterized. This thermophilic enzyme resembles AHAS III of... more
The first step in branched-chain amino acid biosynthesis is catalyzed by acetohydroxyacid synthase (EC 2.2.1.6). This reaction involves decarboxylation of pyruvate followed by condensation with either an additional pyruvate molecule or... more
AHAS I is an isozyme of acetohydroxyacid synthase which is apparently unique to enterobacteria. It has been known for over 20 years that it has many properties which are quite different from those of the other two enterobacterial AHASs... more
Acetohydroxyacid Synthases (AHASs) have separate small regulatory subunits which specifically activate the catalytic subunits with which they are associated. The binding sites for the inhibitory amino acid(s) (valine or leucine) are in... more
His current research interests include market orientation and other strategic orientations, organizational capabilities, and business performance implications of the resource-based view of the firm.
Abstract: Thermoase-digested flaxseed protein hydrolysate (FPH) samples and ultrafiltration membrane-separated peptide fractions were initially evaluated for in vitro inhibition of angiotensin I-converting enzyme (ACE) and renin... more
Salmon protein hydrolysate ORAC Free radicals Antioxidant properties RP-HPLC peptide fractions Amino acid profile Deboned salmon flesh proteins were digested with three proteases (pepsin, trypsin and chymotrypsin) and the digest passed... more
Blood pressure lowering effects of Australian canola protein hydrolysates in spontaneously hypertensive rats.
Acetohydroxy acid synthase (AHAS) catalyzes the first common step in the biosynthesis pathway of the branch chain amino acids in plants and microorganisms. A great deal of interest has been focused on AHAS since it was identified as the... more
Acetohydroxy acid synthase (EC 4.1.3.18), the first enzyme unique to the biosynthesis of the branched chain amino acids valine, leucine and isoleucine, is the site of action of the two different classes of herbicides, the imidazolinones... more
The imidazolinones, a new chemical class of herbicides, were shown to be uncompetitive inhibitors of acetohydroxyacid synthase from corn. This is the first common enzyme in the biosynthetic pathway for valine, leucine, and isoleucine. The... more
An aqueous polyethylene glycol/salt two-phase system was used to estimate the dissociation constant, K(dis), of the Escherichia coli isoenzyme AHAS III regulatory subunit, ilvH protein, from the feedback inhibitor valine. The amounts of... more
Malaria is a deadly disease killing worldwide hundreds of thousands people each year and the responsible parasite has acquired resistance to the available drug combinations. The four vacuolar plasmepsins (PMs) in Plasmodium falciparum... more
Acetohydroxyacid synthase (AHAS) is the first enzyme in the branched-chain amino acid biosynthesis pathway in bacteria. Bioinformatics analysis revealed that the Mycobacterium tuberculosis genome contains four genes (ilvB1, ilvB2, ilvG... more
Acetohydroxyacid synthase (AHAS) is the first enzyme in the branched-chain amino acid biosynthesis pathway in bacteria. Bioinformatics analysis revealed that the Mycobacterium tuberculosis genome contains four genes (ilvB1, ilvB2, ilvG... more
Acetohydroxyacid synthase (AHAS) is the first enzyme in the branched-chain amino acid biosynthesis pathway in bacteria. Bioinformatics analysis revealed that the Mycobacterium tuberculosis genome contains four genes (ilvB1, ilvB2, ilvG... more
Acetohydroxyacid synthase (AHAS; E.C. 4.1.3.18) is the ®rst enzyme in the biosynthetic pathway of the branched-chain amino acids isoleucine, leucine and valine. It is a thiamin diphosphate-dependent enzyme which catalyses the... more
Mechanically-deboned cod muscle proteins were sequentially hydrolysed using pepsin and a trypsin + chymotrypsin combination, which was followed by passing the digest through a 1 kDa equipped tangential flow filtration system; the permeate... more
Biochemical characterization of acetohydroxyacid synthase (EC 4.1.3.18) has been carried out in Daucus carota L. cell cultures, in both wild type and those selected for chlorsulfuron resistance. Two forms of acetohydroxyacid synthase... more
The acetohydroxyacid synthase (AHAS), which is involved in the biosynthesis of branched-chain amino acids (BCAAs), is the target of several classes of herbicides. The catalytic (CSU) and regulatory subunits (RSU) of Mycobacterium... more
The acetohydroxyacid synthase (AHAS), which is involved in the biosynthesis of branched-chain amino acids (BCAAs), is the target of several classes of herbicides. The catalytic (CSU) and regulatory subunits (RSU) of Mycobacterium... more
Thiamin (vitamin B1) is required in animal diets because it is the precursor of the enzyme cofactor, thiamin diphosphate. Unlike other B vitamins, the dietary thiamin requirement is proportional to non-fat energy intake but there is no... more
Acetohydroxyacid synthase (AHAS) is the first common enzyme in the pathway for the biosynthesis of branched-chain amino acids. Interest in the enzyme has escalated over the past 20 years since it was discovered that AHAS is the target of... more
Acetohydroxyacid synthase (AHAS) is the first common enzyme in the pathway for the biosynthesis of branched-chain amino acids. Interest in the enzyme has escalated over the past 20 years since it was discovered that AHAS is the target of... more
Bioactive peptides are short amino acid sequences, that upon release from the parent protein may play different physiological roles, including antioxidant, antihypertensive, antimicrobial, and other bioactivities. They have been identifi... more
Acetohydroxyacid synthase (AHAS) catalyzes the production of acetolactate from pyruvate. The enzyme from the hyperthermophilic bacterium Thermotoga maritima has been purified and characterized (k cat $ 100 s À 1). It was found that the... more
An aqueous polyethylene glycol/salt two-phase system was used to estimate the dissociation constant, K(dis), of the Escherichia coli isoenzyme AHAS III regulatory subunit, ilvH protein, from the feedback inhibitor valine. The amounts of... more
Acetohydroxy acid synthase (AHAS, EC 2.2.1.6; also known as acetolactate synthase, ALS) catalyzes the first common step in the biosynthesis of valine, leucine, and isoleucine in plants and microorganisms. AHAS is the target of several... more