Results 231 to 240 of about 1,936,726 (258)

Substrate specificity of squalene synthetase

Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1980
22 artificial homologues of farnesyl pyrophosphate were examined for the reactivity as substrate for squalene synthetase of pig liver microsomes. 16 of the homologues were found to be reactive to give corresponding squalene-like products. Extention of the omega-terminal of the carbon chain of farnesyl pyrophosphate is acceptable to the enzyme at least ...
T, Koyama, K, Ogura, S, Seto
openaire   +2 more sources

Substrate specificity of polyphenol oxidase

Critical Reviews in Biochemistry and Molecular Biology, 2020
The ubiquitous type-3 copper enzyme polyphenol oxidase (PPO) has found itself the subject of profound inhibitor research due to its role in fruit and vegetable browning and mammalian pigmentation. The enzyme itself has also been applied in the fields of bioremediation, biocatalysis and biosensing.
Mark-Anthony, McLarin, Ivanhoe K H, Leung   +1 more
openaire   +2 more sources

Substrate specificity of pancreatic lipase

Biochimica et Biophysica Acta (BBA) - Enzymology, 1968
Abstract 1. 1. The hydrolysis of esters of oleic acid by pancreatic lipase (glycerol-ester hydrolase, EC 3.1.1.3) depends on the nature of the alcohol. Two factors appear to influence the speed of the reaction: an inductive effect, and steric hindrance. 2. 2.
openaire   +2 more sources

Substrate specificity of vertebrate collagenase

Biochimica et Biophysica Acta (BBA) - Enzymology, 1976
Substrate specificity of purified tadpole collagenase (EC 3.4.24.3) has been studied using eleven synthetic peptides. A pentapeptide, t-butyloxycarbonylprolylalanylglycylisoleucylalanine amide, was susceptible to the action of the enzyme and an octapeptide, acetylprolylglutaminylglycylisoleucylalanylglycylglutaminylarginine ethyl ester, was proposed to
Y, Nagai, Y, Masui, S, Sakakibara
openaire   +2 more sources

Substrate specificity of muscle aldolase

Biochimica et Biophysica Acta, 1954
A study of the substrate specificity of rabbit muscle aldolase led to the following observations. 1. 1. Both the d and l isomers of glyceraldehyde-3-phosphate can be condensed with dihydroxylacetone phospahte, but the former appears to react much more rapidly than the latter. 2. 2. Tagatose-i, 6-diphosphate, which possesses a cis configuration
T C, TUNG, K H, LING, W L, BYRNE, H A, LARDY   +3 more
openaire   +2 more sources

Substrate specificity of adenovirus protease

Virus Research, 2002
The adenovirus protease, adenain is functionally required for virion uncoating and virion maturation and release from the infected cell. In addition to hydrolysis of precursor proteins at specific consensus sites, adenain has also been observed to cleave viral proteins at other sites. Here we re-examine the sequences in the consensus sites and also the
Angelique, Ruzindana-Umunyana, Lise, Imbeault, Joseph M, Weber   +2 more
openaire   +2 more sources

Computation of enzyme-substrate specificity

Biochemistry, 1981
The present study reports the development of a new procedure for teh theoretical computation of enzyme-substrate specificities. The immediate goal has been to identify experimental data with which computations may be effectively compared, examine the underlying theoretical principles, and demonstrate feasibility.
openaire   +2 more sources

On the substrate specificity of glucose oxidase

Biochimica et Biophysica Acta, 1957
Peer ...
Sols, Alberto, Fuente Sánchez, Gertrudis de la   +1 more
openaire   +3 more sources

Substrate specificity of strictosidine synthase

Bioorganic & Medicinal Chemistry Letters, 2006
Strictosidine synthase catalyzes a Pictet-Spengler reaction in the first step in the biosynthesis of terpene indole alkaloids to generate strictosidine. The substrate requirements for strictosidine synthase are systematically and quantitatively examined and the enzymatically generated compounds are processed by the second enzyme in this biosynthetic ...
McCoy, E, Galan , MC, O'Connor, SE
openaire   +4 more sources

Substrate specificity of formylglycinamidine synthetase

Biochemistry, 1986
Formylglycinamidine ribonucleotide (FGAM) synthetase, which catalyzes the conversion of formylglycinamide ribonucleotide (FGAR), glutamine, and ATP to FGAM, ADP, glutamate, and Pi, has been purified to homogeneity (sp act. 0.20 mumol min-1 mg-1) from chicken liver by an alternative procedure to that of Buchanan et al. [Buchanan, J.
F J, Schendel, J, Stubbe
openaire   +2 more sources