S. A. Ahmed

Publications18
h-index5
Citations143
Highly Influential Citations3
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Properties of α-Amino-ε-caprolactam Racemase from Achromobacter obae
α-Amino-e-caprolactam racemase, which occurs in the cytoplasmic fraction of Achromobacter obae, has been purified to homogeneity. It has a monomeric structure with a molecular weight of approximately… Expand
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Racemization of α-Amino-δ-valerolactam Catalyzed by α-Aminog-ε-caprolactam Racemase from Achromobacter obae
(1983). Racemization of α-Amino-δ-valerolactam Catalyzed by α-Amino-∊-caprolactam Racemase from Achromobacter obae. Agricultural and Biological Chemistry: Vol. 47, No. 5, pp. 1149-1150.
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[49] Tryptophan synthase from Escherichia coli and Salmonella typhimurium
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The Cellular Transport of Magnesium in Rat Liver
The bidirectional transport of Mg in rat liver was studied using slices labeled with 28Mg in a closed two-compartment system under steady-state conditions. The influx (Kbs) and efflux (Ksb) transfer… Expand
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L‐α‐Amino‐β‐thio‐ϵ‐caprolactam, a new sulfur‐containing Substrate for α‐amino‐ϵ‐caprolactam racemase
A one‐step synthesis of a new sulfur‐containing compound, L‐α‐amino‐β‐thio‐ϵ‐caprolactam from L‐cysteine methyl ester and 2‐chloroethylamine has been described. This intramolecular cyclic amide of… Expand
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Mechanism of α-amino-ε-caprolactam racemase reaction
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THE STREPTOCOCCAL NADH PEROXIDASE AND NADH OXIDASE: STRUCTURAL AND MECHANISTIC ASPECTS
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Mechanism of Inactivation of α-Amino-ε-caprolactam Racemase by α-Amino-δ -valerolactam
Both D- and L-α-amino-δ-valerolactam inactivated α-amino-e-caprolactam racemase during incubation with the enzyme. The degree of inactivation increased with increases in pH and the concentration of… Expand
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ARTIFICIAL FLAVINS AS PROBES OF THE ACTIVE-SITE ENVIRONMENT AND REDOX BEHAVIOR OF THE STREPTOCOCCAL NADH PEROXIDASE
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THE STRUCTURE OF NADH PEROXIDASE FROM STREPTOCOCCUS FAECALIS
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