Enoyl-ACP Reductase (FabI) of Haemophilus influenzae: Steady-State Kinetic Mechanism and Inhibition by Triclosan and Hexachlorophene

2001 ◽  
Vol 396 (2) ◽  
pp. 249
Author(s):  
Jovita Marcinkeviciene ◽  
Wenjun Jiang ◽  
Lisa M. Kopcho ◽  
Gregory Locke ◽  
Ying Luo ◽  
...  
Keyword(s):  
Steady State ◽  
Haemophilus Influenzae ◽  
Kinetic Mechanism ◽  
Steady State Kinetic ◽  
Enoyl Acp Reductase ◽  
State Kinetic

Enoyl-ACP Reductase (FabI) of Haemophilus influenzae: Steady-State Kinetic Mechanism and Inhibition by Triclosan and Hexachlorophene

2001 ◽  
Vol 390 (1) ◽  
pp. 101-108 ◽  
Author(s):  
Jovita Marcinkeviciene ◽  
Wenjun Jiang ◽  
Lisa M Kopcho ◽  
Gregory Locke ◽  
Ying Luo ◽  
...  
Keyword(s):  
Steady State ◽  
Haemophilus Influenzae ◽  
Kinetic Mechanism ◽  
Steady State Kinetic ◽  
Enoyl Acp Reductase ◽  
State Kinetic

scholarly journals Steady-state kinetic mechanism of the NADP+- and NAD+-dependent reactions catalysed by betaine aldehyde dehydrogenase from Pseudomonas aeruginosa

2000 ◽  
Vol 352 (3) ◽  
pp. 675-683 ◽  
Author(s):  
Roberto VELASCO-GARCÍA ◽  
Lilian GONZÁLEZ-SEGURA ◽  
Rosario A. MUÑOZ-CLARES
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Steady State ◽  
Aldehyde Dehydrogenase ◽  
Substrate Inhibition ◽  
Kinetic Mechanism ◽  
Betaine Aldehyde Dehydrogenase ◽  
Betaine Aldehyde ◽  
Metabolic Role ◽  
Steady State Kinetic ◽  
State Kinetic

Betaine aldehyde dehydrogenase (BADH) catalyses the irreversible oxidation of betaine aldehyde to glycine betaine with the concomitant reduction of NAD(P)+ to NADP(H). In Pseudomonas aeruginosa this reaction is a compulsory step in the assimilation of carbon and nitrogen when bacteria are growing in choline or choline precursors. The kinetic mechanisms of the NAD+- and NADP+-dependent reactions were examined by steady-state kinetic methods and by dinucleotide binding experiments. The double-reciprocal patterns obtained for initial velocity with NAD(P)+ and for product and dead-end inhibition establish that both mechanisms are steady-state random. However, quantitative analysis of the inhibitions, and comparison with binding data, suggest a preferred route of addition of substrates and release of products in which NAD(P)+ binds first and NAD(P)H leaves last, particularly in the NADP+-dependent reaction. Abortive binding of the dinucleotides, or their analogue ADP, in the betaine aldehyde site was inferred from total substrate inhibition by the dinucleotides, and parabolic inhibition by NADH and ADP. A weak partial uncompetitive substrate inhibition by the aldehyde was observed only in the NADP+-dependent reaction. The kinetics of P. aeruginosa BADH is very similar to that of glucose-6-phosphate dehydrogenase, suggesting that both enzymes fulfil a similar amphibolic metabolic role when the bacteria grow in choline and when they grow in glucose.

scholarly journals Steady-State Kinetic Analysis of Phosphotransacetylase from Methanosarcina thermophila

2006 ◽  
Vol 188 (3) ◽  
pp. 1155-1158 ◽  
Author(s):  
Sarah H. Lawrence ◽  
James G. Ferry
Keyword(s):  
Steady State ◽  
Kinetic Analysis ◽  
Random Order ◽  
Kinetic Mechanism ◽  
Methanosarcina Thermophila ◽  
Steady State Kinetic ◽  
Ping Pong ◽  
Acetyl Group ◽  
State Kinetic ◽  
Reversible Transfer

ABSTRACT Phosphotransacetylase (EC 2.3.1.8) catalyzes the reversible transfer of the acetyl group from acetyl phosphate to coenzyme A (CoA), forming acetyl-CoA and inorganic phosphate. A steady-state kinetic analysis of the phosphotransacetylase from Methanosarcina thermophila indicated that there is a ternary complex kinetic mechanism rather than a ping-pong kinetic mechanism. Additionally, inhibition patterns of products and a nonreactive substrate analog suggested that the substrates bind to the enzyme in a random order. Dynamic light scattering revealed that the enzyme is dimeric in solution.

Steady-State Kinetic Mechanism and Reductive Half-Reaction ofd-Arginine Dehydrogenase fromPseudomonas aeruginosa

Biochemistry ◽  
2010 ◽  
Vol 49 (44) ◽  
pp. 9542-9550 ◽  
Author(s):  
Hongling Yuan ◽  
Guoxing Fu ◽  
Phillip T. Brooks ◽  
Irene Weber ◽  
Giovanni Gadda
Keyword(s):  
Steady State ◽  
Kinetic Mechanism ◽  
Steady State Kinetic ◽  
State Kinetic

scholarly journals Steady-state Kinetic Mechanism of PDK1

2006 ◽  
Vol 281 (31) ◽  
pp. 21670-21681 ◽  
Author(s):  
Xinxin Gao ◽  
Thomas K. Harris
Keyword(s):  
Steady State ◽  
Kinetic Mechanism ◽  
Steady State Kinetic ◽  
State Kinetic

Steady-State Kinetic Mechanism of Escherichia coli UDP-N-Acetylenolpyruvylglucosamine Reductase

Biochemistry ◽  
1995 ◽  
Vol 34 (16) ◽  
pp. 5390-5402 ◽  
Author(s):  
Adil M. Dhalla ◽  
Joseph Yanchunas ◽  
Hsu-Tso Ho ◽  
Paul Falk ◽  
Joseph J. Villafranca ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Steady State ◽  
Kinetic Mechanism ◽  
Steady State Kinetic ◽  
State Kinetic
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