2008
DOI: 10.1107/s090744490801411x
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1.6 Å structure of an NAD+-dependent quinate dehydrogenase fromCorynebacterium glutamicum

Abstract: To date, three different functional classes of bacterial shikimate/quinate dehydrogenases have been identified and are referred to as AroE, SDH-L and YdiB. The enzyme AroE and the catalytically much slower SDH-L clearly prefer NADP+/NADPH as the cosubstrate and are specific for (dehydro-)shikimate, whereas in YdiB the differences in affinity for NADP+/NADPH versus NAD+/NADH as well as for (dehydro-)shikimate versus (dehydro-)quinate are marginal. These three subclasses have a similar three-dimensional fold and… Show more

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Cited by 9 publications
(12 citation statements)
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“…The arrangement of these two domains creates a deep groove, in which the cofactor and substrate are located, and forms the active site. The CglQSDH appears to exist as dimer in solution as we reported previously (Schoepe et al, 2006(Schoepe et al, , 2008.…”
Section: Structure Overview Of C Glutamicum Qsdhsupporting
confidence: 78%
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“…The arrangement of these two domains creates a deep groove, in which the cofactor and substrate are located, and forms the active site. The CglQSDH appears to exist as dimer in solution as we reported previously (Schoepe et al, 2006(Schoepe et al, , 2008.…”
Section: Structure Overview Of C Glutamicum Qsdhsupporting
confidence: 78%
“…The protein parts of the three complex structures reported here and of the apo-CglQSDH published previously (Schoepe et al, 2008) are largely identical; they possess the two-domain architecture typical for members of the SDH/QDH protein family consisting of an N-terminal catalytic or substrate-binding domain and a C-terminal or nucleotide-binding domain.…”
Section: Structure Overview Of C Glutamicum Qsdhmentioning
confidence: 64%
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“…A total of 20 crystal structures of SDH have been determined so far covering all the three orthologues of SDH mentioned above, including AroE from E. coli (PDB code: 1NYT [9]), H. influenzae (1P74 and 1P77 [10]), Methanococcus jannaschii (1NVT [11]), Aquifex aeolicus (2HK7, 2HK8 and 2HK9 [12]), Thermus thermophilus (1WXD, 2CY0, 2D5C and 2EV9 [13]), Arabidopsis thaliana (2GPT [14], 2O7Q and 2O7S [15]) and Geobacillus kaustophilus (2EGG); YdiB from E. coli (1O9B [9], 1NPD [16] and 1VI2) and Corynebacterium glutamicum (2NLO [17]); and SDHL from H. influenzae (1NPY [8]). These structures comprise the following diverse conformations (a) apo‐enzyme (1NPY, 1P74, 1WXD, 2EGG, 2HK7, 2HK8 and 2NLO), (b) binary complex bound with either cofactor (1NPD, 1NVT, 1NYT, 1O9B, 1P77, 1VI2 and 2CY0) or substrate (2D5C, 2GPT and 2O7Q) and (c) inactive (2HK9_A and 2EV9) and active (2HK9_D and 2O7S) ternary complexes.…”
mentioning
confidence: 99%
“…On the other hand, it is likely that the enzyme involved in the catabolic role acts on both quinate and shikimate as substrates and prefers NAD as a coenzyme in fungi and gram-positive bacteria, although genetic characterization of the bacterial enzymes is obscure (3,12,14). Recently, a product of the C. glutamicum ATCC 13032 cgl0424 gene, corresponding to the product of qsuD of C. glutamicum R (99% amino acid sequence identity), was overexpressed in E. coli, purified, and characterized, and the three-dimensional structure was determined (33). The results indicate that the enzyme prefers quinate and NAD, although its physiological function has not been clarified.…”
Section: Vol 75 2009mentioning
confidence: 99%