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1 tal structure of an irreversibly inactivated proline dehydrogenase.
2 iptional repressor and a membrane-associated proline dehydrogenase.
3 X closely resembles the alphabeta dimer of L-proline dehydrogenase, a heteroctameric protein (alphabe
4 e involved in transmitting the status of the proline dehydrogenase active site and flavin redox state
7 of Delta1-pyrroline-5-carboxylate synthase, proline dehydrogenase and 9-cis-epoxycarotenoid dioxygen
8 L-glutamate by the sequential activities of proline dehydrogenase and aldehyde dehydrogenase domains
9 loci for the amino acid-metabolizing enzymes proline dehydrogenase and alpha-aminoadipic semialdehyde
10 enzyme that contains the DUF in addition to proline dehydrogenase and l-glutamate-gamma-semialdehyde
11 proteins such as succinate dehydrogenase and proline dehydrogenase, and alleviation of inhibition of
12 orter, LutABC lactate dehydrogenase and PutA proline dehydrogenase became more abundant with increasi
16 hat residues of the beta3-alpha3 loop of the proline dehydrogenase domain (betaalpha)8 barrel are inv
21 resolution structure of Thermus thermophilus proline dehydrogenase inactivated by the mechanism-based
22 cterium tumefaciens putA gene, which encodes proline dehydrogenase, is transcriptionally induced by e
23 nsistently, expression of both of the poplar Proline Dehydrogenase orthologs and two of the Flavonol
24 effect of proline was blocked by concomitant proline dehydrogenase/oxidase (PRODH/POX) knockdown.
25 carboxylate synthetase (P5CS) and decreasing proline dehydrogenase (PDH) activity, while Si reversed
26 pherally membrane-bound enzyme that has both proline dehydrogenase (PDH) and Delta(1)-pyrroline-5-car
27 osmolytes (pyrroline-5-carboxylate synthase, proline dehydrogenase (PDH), betaine aldehyde dehydrogen
28 F15, aminoacid catabolizing enzymes, notably proline dehydrogenase (POX), and adipose triglyceride li
30 ave shown that the binding of proline in the proline dehydrogenase (PRODH) active site and subsequent
31 the candidate risk genes encode the enzymes proline dehydrogenase (PRODH) and catechol-O-methyltrans
32 ization A (PutA) flavoenzyme, which contains proline dehydrogenase (PRODH) and Delta(1)-pyrroline-5-c
33 A) is a large bifunctional flavoenzyme with proline dehydrogenase (PRODH) and Delta(1)-pyrroline-5-c
35 ding protein to a membrane-bound enzyme with proline dehydrogenase (PRODH) and Delta(1)-pyrroline-5-c
37 ation of proline to glutamate using separate proline dehydrogenase (PRODH) and l-glutamate-gamma-semi
38 oxidation of L-proline to L-glutamate using proline dehydrogenase (PRODH) and L-glutamate-gamma-semi
39 a the sequential activities of FAD-dependent proline dehydrogenase (PRODH) and NAD(+)-dependent Delta
43 revious crystallographic studies of the PutA proline dehydrogenase (PRODH) domain under oxidizing con
45 ccumulation in turn stimulated expression of proline dehydrogenase (PRODH) which resulted in mitochon
46 eport the characterization of a bifunctional proline dehydrogenase (PutA(669)) that contains residues
47 elanogaster sluggish-A (slgA), which encodes proline dehydrogenase responsible for the behavioural ph
48 of SmPutA with a proline analog bound to the proline dehydrogenase site and NAD(+) bound to the ALDH
50 romosome 22q11.2, located in and near PRODH (proline dehydrogenase), were associated with L-proline i
51 the homologous arcB and ocd genes, and (iv) proline dehydrogenase, which converts proline to glutama