A. S. Alhomida

King Saud University, Biochemistry, Faculty Member

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I am currently working in the area of carnitine metabolism, metabolic biomarkers, hydroxyproline, collagen metabolism and the effect of renal hemodialysis on the metabolic concentrations found in Saudi chronic renal failure patients. Additionally, I am involved with several other projects, including studies into enzyme kinetics and mechanisms, renal disease, heart diseases, Alzheimer's disease, nanoparticles, anticancer drugs, antimalarial drugs, heart disease and eye disease. I am also studying the role of the carnitine pathway of energy metabolism in the Arabian camel (Camelus dromedarius), in order to explore the relationship between carnitine and the camel's superior ability to subsist in the harsh desert climate compared to other animals.
Supervisors: Professor Daniel J. Smith
Phone: (+966-1) 469-3820
Address: Vice Dean for Graduate Studies and Scientific Research
Dept of Biochemistry
King Saud University
119 King Abdullah Rd
Bldg 5, Office 2A 62
POB 2455, Riyadh 11451
SAUDI ARABIA

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Badreldin Ali

Sultan Qaboos University

Dr. Muhammad Yaqoob

University of Agriculture, Faisalabad, Pakistan

Alkali Haruna

Federal University Kashere, Gombe State, Nigeria

Wasfy Rahman

Independent University, Bangladesh

Faisel Mohamed

MIsr higher institute of engineering and technology

King Saud University

Desert Research Center (DRC)

Saeed Nazifi

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Books by A. S. Alhomida

Mechanisms of Enzyme Action (Unpublished)

Papers by A. S. Alhomida

Kinetic properties of purified carnitine acetyltransferase from the skeletal muscle of Arabian camel ( Camelus dromedarius

Biochimie, 1996

The kinetic properties of carnitine acetyltransferase from the skeletal muscle of the Arabian cam... more The kinetic properties of carnitine acetyltransferase from the skeletal muscle of the Arabian camel (Camelus dromedarius) were studied. The enzyme showed an optimum pH between 7.2 and 8.2. Reciprocal plots of data obtained by varying one substrate concentration while keeping the other constant revealed lines that converged on the abscissa, indicating that the enzyme possible follows a random mechanism of catalysis. The Kms for L-carnitine and acetyl-coenzyme A were 244 and 44 microM respectively, while those for acetyl-DL-carnitine and coenzyme A (Co A) were 307 and 39 microM respectively. The Km for one substrate was found to be independent of the concentration of the second substrate used. Corresponding Vmax values for L-CA, acetyl-Co A, acetyl-DL-carnitine and Co A are 98, 98, 102 and 100 mumol min-1 mg-1 protein respectively. The low Km obtained for acetyl-DL-carnitine suggests an adaptive mechanism in this desert species for enduring prolonged dry spells without food and water.

Purification and characterization of acetylcholinesterase from desert cobra ( Walterinnesia aegyptia) venom

Biochimie, 1996

Acetyl-CoA hydrolase, which hydrolyzes acetyl-CoA to acetate and CoASH, was isolated from Succhur... more Acetyl-CoA hydrolase, which hydrolyzes acetyl-CoA to acetate and CoASH, was isolated from Succhuromycrs cerevisiae and demonstrated by protein sequence analysis to be NH2-terminally blocked. The enzyme was purified 3 080-fold to apparent homogeneity by successive purification steps using DEAE-Sepharose, gel filtration and hydroxylapatite. The molecular mass of the native yeast acetyl-CoA hydrolase was estimated to be 64 f 5 kDa by gel-filtration chromatography. SDSjPAGE analysis revealed that the denatured molecular mass was 65 f 2 kDa and together with that for the native enzyme indicates that yeast acetyl-CoA hydrolase was monomeric. The enzyme had a pH optimum near 8.0 and its PI was approximately 5.8. Several acyl-CoA derivatives of varying chain length were tested as substrates for yeast acetyl-CoA hydrolase. Although acetyl-CoA hydrolase was relatively specific for acetyl-CoA, longer acyl-chain CoAs were also hydrolyzed and were capable of functioning as inhibitors during the hydrolysis of acetyl-CoA. Among a series of divalent cations, Zn2+ was demonstrated to be the most potent inhibitor. The enzyme was inactivated by chemical modification with diethyl pyrocarbonate, a histidine-modifying reagent.

A. S. Alhomida

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