Study of Two Alanine Racemases From Sal. Typhimurium

Faraci, W S.

Abstract

Funding Agency

• Agency: National Institute of Health (NIH)
• Institute: National Institute of General Medical Sciences (NIGMS)
• Type: Postdoctoral Individual National Research Service Award (F32)
• Project #: 7F32GM011471-02
• Application #: 3041864
• Study Section: (BI)
• Project Start: 1987-10-01
• Project End: 1988-09-30
• Budget Start: 1987-10-01
• Budget End: 1988-09-30
• Support Year: 2
• Fiscal Year: 1987

Institution

• Name: Harvard University
• Type: Schools of Medicine
• DUNS #: 082359691
• City: Boston
• State: MA
• Country: United States
• Zip Code: 02115

Publications

Duncan, K; Faraci, W S; Matteson, D S et al. (1989) (1-Aminoethyl)boronic acid: a novel inhibitor for Bacillus stearothermophilus alanine racemase and Salmonella typhimurium D-alanine:D-alanine ligase (ADP-forming). Biochemistry 28:3541-9

Rusnak, F; Faraci, W S; Walsh, C T (1989) Subcloning, expression, and purification of the enterobactin biosynthetic enzyme 2,3-dihydroxybenzoate-AMP ligase: demonstration of enzyme-bound (2,3-dihydroxybenzoyl)adenylate product. Biochemistry 28:6827-35

Faraci, W S; Walsh, C T (1989) Mechanism of inactivation of alanine racemase by beta, beta, beta-trifluoroalanine. Biochemistry 28:431-7

Copie, V; Faraci, W S; Walsh, C T et al. (1988) Inhibition of alanine racemase by alanine phosphonate: detection of an imine linkage to pyridoxal 5'-phosphate in the enzyme-inhibitor complex by solid-state 15N nuclear magnetic resonance. Biochemistry 27:4966-70

Faraci, W S; Walsh, C T (1988) Racemization of alanine by the alanine racemases from Salmonella typhimurium and Bacillus stearothermophilus: energetic reaction profiles. Biochemistry 27:3267-76