Preliminary crystallographic analysis of L-2-keto-3-deoxyarabonate dehydratase, an enzyme involved in an alternative bacterial pathway of L-arabinose metabolism.
L-2-Keto-3-deoxyarabonate (L-KDA) dehydratase is a novel member of the dihydrodipicolinate synthase (DHDPS)/N-acetylneuraminate lyase (NAL) protein family and catalyzes the hydration of L-KDA to alpha-ketoglutaric semialdehyde. L-KDA dehydratase was overexpressed, purified and crystallized at 291 K using the hanging-drop vapour-diffusion method. The crystal diffracts to 2.0 A resolution using synchrotron radiation and belongs to the trigonal space group P3(1)21 or its enantiomorph P3(2)21, with unit-cell parameters a = b = 78.91, c = 207.71 A.
Shimada
Naoko
N
Institute of Advanced Energy, Kyoto University, Gokasyo, Uji, Kyoto 611-0011, Japan.
Mikami
Bunzo
B
Watanabe
Seiya
S
Makino
Keisuke
K
D000595:Amino Acid Sequence; D001089:Arabinose / Q000378:metabolism*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology*; D006836:Hydro-Lyases / Q000737:chemistry*; D011487:Protein Conformation
D001089:Arabinose; D006836:Hydro-Lyases; C521234:L-2-keto-3-deoxyarabonate dehydratase, Azospirillum brasilense