scholarly journals Insights into substrate specificity, regioselectivity and mechanism of two fatty acid hydratases from Lactobacillus acidophilus from mutational and kinetic studies

2021 ◽  
Author(s):  
Bekir Engin Eser ◽  
Yan Zhang ◽  
Michal Poborsky ◽  
Negin Hashemi ◽  
Sune Schubert ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Substrate Specificity ◽  
Lactobacillus Acidophilus ◽  
Kinetic Studies

Kinetic Studies, Mechanism, and Substrate Specificity of Amadoriase I fromAspergillus sp.†

Biochemistry ◽  
2001 ◽  
Vol 40 (43) ◽  
pp. 12886-12895 ◽  
Author(s):  
Xinle Wu ◽  
Bruce A. Palfey ◽  
Valeri V. Mossine ◽  
Vincent M. Monnier
Keyword(s):  
Substrate Specificity ◽  
Kinetic Studies

scholarly journals Kinetic studies on pancreatic lipase activity in micellar systems. II. Effect of fatty acid chain length of substrates.

1983 ◽  
Vol 31 (12) ◽  
pp. 4213-4219 ◽  
Author(s):  
HIROSHI NAKAHARA ◽  
SATOSHI OKADA ◽  
KENSHU MOCHIDA ◽  
HIDENOBU OHMORI ◽  
MASAICHIRO MASU
Keyword(s):  
Fatty Acid ◽  
Chain Length ◽  
Pancreatic Lipase ◽  
Lipase Activity ◽  
Kinetic Studies ◽  
Fatty Acid Chain Length ◽  
Fatty Acid Chain ◽  
Micellar Systems

Optimisation and Kinetic Studies of Acid Esterification of High Free Fatty Acid Rubber Seed Oil

2015 ◽  
Vol 41 (7) ◽  
pp. 2515-2526 ◽  
Author(s):  
Lai Fatt Chuah ◽  
Awais Bokhari ◽  
Suzana Yusup ◽  
Jiří Jaromír Klemeš ◽  
Bawadi Abdullah ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Free Fatty Acid ◽  
Seed Oil ◽  
Kinetic Studies ◽  
High Free Fatty Acid ◽  
Rubber Seed Oil ◽  
Rubber Seed ◽  
Acid Esterification

scholarly journals Plastidic Δ6 Fatty-Acid Desaturases with Distinctive Substrate Specificity Regulate the Pool of C18-PUFAs in the Ancestral Picoalga Ostreococcus tauri

2020 ◽  
Vol 184 (1) ◽  
pp. 82-96
Author(s):  
Charlotte Degraeve-Guilbault ◽  
Rodrigo E. Gomez ◽  
Cécile Lemoigne ◽  
Nattiwong Pankansem ◽  
Soizic Morin ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Substrate Specificity ◽  
Fatty Acid Desaturases ◽  
Ostreococcus Tauri

scholarly journals The enzymology of short-chain fatty acyl-coenzyme A synthetase from seeds of Pinus radiata. Kinetic studies and a proposed reaction mechanism

1974 ◽  
Vol 137 (3) ◽  
pp. 435-442 ◽  
Author(s):  
Owen A. Young ◽  
John W. Anderson
Keyword(s):  
Fatty Acid ◽  
Pinus Radiata ◽  
Kinetic Studies ◽  
Single Species ◽  
Competitive Inhibitor ◽  
Fatty Acyl ◽  
Short Chain ◽  
Low Concentrations ◽  
High Concentrations ◽  
Acyl Coenzyme A

1. Short-chain fatty acyl-CoA synthetase from seeds of Pinus radiata was examined by acetate- and propionate-dependent PPi–ATP exchange. Reaction mixtures came to equilibrium almost instantly as judged by rates of exchange and analysis of an incubation mixture. 2. The activity of the enzyme was correlated with the concentration of MgP2O72- but not with the concentration of Mg2+, as judged by PPi–ATP exchange and fatty acyl AMP-dependent synthesis of ATP in the presence of PPi. In PPi–ATP exchange assays, no clear relationship between activity and any single species of ATP was apparent. 3. High concentrations of fatty acid inhibited PPi–ATP exchange. PPi–dATP exchange was less than PPi–ATP exchange at low concentrations of fatty acid, but at higher concentrations PPi–dATP exchange exceeded PPi–ATP exchange. The rate of synthesis of fatty acyl-CoA in the presence of dATP was less than with ATP. 4. ATP and propionate inhibited the synthesis of ATP from propionyl-AMP and PPi. The inhibition by ATP was competitive with respect to propionyl-AMP and non-competitive with respect to PPi. The inhibition by propionate was non-competitive with respect to propionyl-AMP and PPi. 5. AMP was a competitive inhibitor of propionyl-AMP-dependent synthesis of ATP and competitively inhibited propionate-dependent PPi–ATP exchange when ATP was the variable substrate. 6. It was concluded that the first partial reaction catalysed by the enzyme is ordered; ATP is the first substrate to react with the enzyme and PPi is probably the only product released.

scholarly journals Rational Engineering of Hydratase from Lactobacillus acidophilus Reveals Critical Residues Directing Substrate Specificity and Regioselectivity

ChemBioChem ◽  
2019 ◽  
Vol 21 (4) ◽  
pp. 550-563 ◽  
Author(s):  
Bekir Engin Eser ◽  
Michal Poborsky ◽  
Rongrong Dai ◽  
Shigenobu Kishino ◽  
Anita Ljubic ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Lactobacillus Acidophilus ◽  
Rational Engineering ◽  
Critical Residues

Substrate specificity and kinetic studies on thiogalactoside transacetylase

Biochemistry ◽  
1973 ◽  
Vol 12 (3) ◽  
pp. 553-557 ◽  
Author(s):  
Richard E. Musso ◽  
Irving Zabin
Keyword(s):  
Substrate Specificity ◽  
Kinetic Studies
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