Kinetic and structural characterization for cofactor preference of succinic semialdehyde dehydrogenase from Streptococcus pyogenes.
Kinetic and structural characterization for cofactor preference of succinic semialdehyde dehydrogenase from Streptococcus pyogenes.
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DOI：
10.14348/molcells.2014.0162
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发表时间：
2014-10-31
影响因子：
3.8
通讯作者：
Lee KS
中科院分区：
文献类型：
--
作者：
Jang EH;Park SA;Chi YM;Lee KS
The γ-Aminobutyric acid (GABA) that is found in prokaryotic and eukaryotic organisms has been used in various ways as a signaling molecule or a significant component generating metabolic energy under conditions of nutrient limitation or stress, through GABA catabolism. Succinic semialdehyde dehydrogenase (SSADH) catalyzes the oxidation of succinic semialdehyde to succinic acid in the final step of GABA catabolism. Here, we report the catalytic properties and two crystal structures of SSADH from Streptococcus pyogenes (SpSSADH) regarding its cofactor preference. Kinetic analysis showed that SpSSADH prefers NADP+ over NAD+ as a hydride acceptor. Moreover, the structures of SpSSADH were determined in an apo-form and in a binary complex with NADP+ at 1.6 Å and 2.1 Å resolutions, respectively. Both structures of SpSSADH showed dimeric conformation, containing a single cysteine residue in the catalytic loop of each subunit. Further structural analysis and sequence comparison of SpSSADH with other SSADHs revealed that Ser158 and Tyr188 in SpSSADH participate in the stabilization of the 2’-phosphate group of adenine-side ribose in NADP+. Our results provide structural insights into the cofactor preference of SpSSADH as the gram-positive bacterial SSADH.
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影响因子：
5.8
作者：
Gouet, P;Courcelle, E;Métoz, F
通讯作者：
Métoz, F
DOI：
10.1107/s0907444904019158
发表时间：
2004-12-01
影响因子：
2.2
作者：
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通讯作者：
Cowtan, K
影响因子：
3.2
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影响因子：
3.2
作者：
Chaussee, MA;Callegari, EA;Chaussee, MS
通讯作者：
Chaussee, MS
影响因子：
3.9
作者：
de Carvalho LP;Ling Y;Shen C;Warren JD;Rhee KY
通讯作者：
Rhee KY