ライフサイエンスコーパス: dehydrase

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1 Our data showed that H220K-E1 has no dehydrase activity, but can act as a PLP-dependent trans

2 reveal that SpnO and SpnN functions as a 2,3-dehydrase and a 3-ketoreductase, respectively.

3 onance (EPR) spectroscopy in samples of diol dehydrase and the functional adenosylcobalamin (AdoCbl)

4 tedness to acyl carrier proteins, fatty acid dehydrases and beta-ketoacylsynthases, respectively, whi

5 e properties of the beta-ketoacyl reductase, dehydrase, and enoyl reductase components of the animal

6 ein domain with the beta-ketoacyl reductase, dehydrase, and enoyl reductase domains associated exclus

7 This compound supports activity for diol dehydrase at 0.02% of that observed with AdoCbl.

8 nce of the substrate indicates that, in diol dehydrase, binding of the coenzyme to the protein weaken

9 ing functional beta-ketoacyl synthase (KS-), dehydrase (DH-), acyl carrier protein (ACP-), or thioest

10 n but are coiled in a manner that allows the dehydrase domain to access the beta-hydroxyacyl-ACP loca

11 These data indicate that the dehydrase domain, although located in the amino-terminal

12 CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase (E(1)) catalyzes the C-3 deoxygenation in the

13 tic analysis of SpnQ and related NDP-sugar 3-dehydrases E1 and ColD are discussed.

14 CDP-6-deoxy-L-threo-D-glycero-4-hexulose 3-dehydrase (E1), along with its reductase (E3), catalyzes

15 CDP-6-deoxy-L-threo-D-glycero-4-hexulose 3-dehydrase (E1), together with its reductase (E3), cataly

16 CDP-6-deoxy-l-threo-d-glycero-4-hexulose-3-dehydrase (E1), which catalyzes C-3 deoxygenation of CDP

17 : CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase (E1), which contains a pyridoxamine and a [2Fe

18 s CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase (E1), which is a pyridoxamine 5'-phosphate dep

19 y CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase (E1), which is PMP-dependent and contains a re

20 subunit containing a mutation in either the dehydrase, enoyl reductase, beta-ketoacyl reductase, or

21 nits carry a knockout mutation in either the dehydrase, enoyl reductase, keto reductase, or acyl carr

22 s, i.e. ketoacyl synthase, acyl transferase, dehydrase, enoyl reductase, ketoreductase and/or ACP.

23 bserved for beta-hydroxydecanoyl thiol ester dehydrase from Escherichia coli.

24 at the equilibrium and rate constant for the dehydrase reaction favor the formation of beta-hydroxy r

25 , CDP-6-deoxy-l-threo-d-glycero-4-hexulose-3-dehydrase reductase (E3), CDP-4-aceto-3,6-dideoxygalacto

26 t CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase reductase (E3), which contains both an FAD and

27 , CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase reductase (E3, formerly known as CDP-6-deoxy-d

28 , CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase reductase, formally called CDP-6-deoxy-delta(3

29 functions as GDP-4-keto-6-deoxy-D-mannose-3-dehydrase responsible for C-3 deoxygenation of GDP-4-ket

30 yl synthase, malonyl/acetyltransacylase, and dehydrase, separated by a 600-residue structural core fr

31 nd F345H, converted E 1 from a PMP-dependent dehydrase to a PLP/glutamate-dependent aminotransferase.

32 bond of anAdoCbl at the active site of diol dehydrase was observed by spectrophotometric detection o

33 idoxamine 5'-monophosphate (PMP)-dependent 3-dehydrase which, in the presence of the cellular reducta

34 bstrate and beta-hydroxydecanoyl thiol ester dehydrase with inhibitor onto the AtFatB model showed th

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