ライフサイエンスコーパス: pyruvate decarboxylase

1 ch, toward converting BFDC into an efficient pyruvate decarboxylase.

2 retic substrate activation behavior of yeast pyruvate decarboxylase.

3 t of other ThDP-dependent enzymes, including pyruvate decarboxylase.

4 hiamin diphosphate- (ThDP-) dependent enzyme pyruvate decarboxylase.

5 ions of directed evolution resulted in yeast pyruvate decarboxylase 1 (Pdc1) variants with improved a

6 We also show that pyruvate decarboxylase (AceE), the E1 component of pyruv

7 Ferredoxin was not necessary for the pyruvate decarboxylase activity of POR, nor did it inhib

8 has been made possible by the evolution of a pyruvate decarboxylase, analogous to that in brewer's ye

9 umption, whereas the enzymatic activities of pyruvate decarboxylase and alcohol dehydrogenase were in

10 t to substrate activation, Zymomonas mobilis pyruvate decarboxylase and benzoylformate decarboxylase.

11 hydrogenase, an RNA-binding protein), Pdc1p (pyruvate decarboxylase), and an unknown approximately 35

12 a coli pyruvate dehydrogenase complex, yeast pyruvate decarboxylase, and pyruvate oxidase from Lactob

13 ng pyruvate oxidase, glyoxylate carboligase, pyruvate decarboxylase, and the acetolactate synthase fo

14 dative decarboxylation to acetyl-CoA via the pyruvate decarboxylase complex or the biotin-dependent c

15 The pyruvate decarboxylase component, a heterotetramer E1(al

16 The enzymes pyruvate decarboxylase (E1) and dihydrolipoyl dehydrogen

17 Pyruvate decarboxylase (E1) catalyzes the first two reac

18 rder to undergo reductive acetylation by the pyruvate decarboxylase (E1) component, in contrast with

19 e heterotetrameric (alpha(2)beta(2)) 153-kDa pyruvate decarboxylase (E1) from Bacillus stearothermoph

20 in the presence of native E3 and recombinant pyruvate decarboxylase (E1).

21 etyltransferase (E2) core component with the pyruvate decarboxylase (E1, alpha2beta2) and dihydrolipo

22 Limited proteolysis of the pyruvate decarboxylase (E1, alpha2beta2) component of th

23 ABCD operon of Bacillus subtilis encodes the pyruvate decarboxylase (E1alpha and E1beta), dihydrolipo

24 arothermophilus, the interaction between the pyruvate decarboxylase (E1p) component and the lipoyl do

25 oli is catalysed specifically by its partner pyruvate decarboxylase (E1p), and no productive interact

26 site-specific mutagenesis was carried out on pyruvate decarboxylase (EC 4.1.1.1) from Saccharomyces c

27 site-specific mutagenesis was carried out on pyruvate decarboxylase (EC 4.1.1.1) from Saccharomyces c

28 site-specific mutagenesis was carried out on pyruvate decarboxylase (EC 4.1.1.1) from Saccharomyces c

29 site-specific mutagenesis was carried out on pyruvate decarboxylase (EC 4.1.1.1) from Saccharomyces c

30 When the E91D variant of apo-yeast pyruvate decarboxylase (EC 4.1.1.1) is exposed to C2alph

31 The crystal structure of pyruvate decarboxylase (EC 4.1.1.1), a thiamin diphospha

32 The residue C221 on pyruvate decarboxylase (EC. 4.1.1.1) from Saccharomyces

33 se properties in the region of pH optimum of pyruvate decarboxylase from Saccharomyces cerevisiae hav

34 The residue I415 in pyruvate decarboxylase from Saccharomyces cerevisiae was

35 Pyruvate decarboxylase from yeast (YPDC, EC 4.1.1.1) exh

36 The pdc1 gene encoding pyruvate decarboxylase has been isolated and sequenced f

37 Substrate activation of yeast pyruvate decarboxylase has been studied extensively in t

38 cose upon expression of a recombinant mutant pyruvate decarboxylase in the RARE strain.

39 Pyruvate decarboxylase is a homotetrameric enzyme which

40 to the E477Q active-center variant of yeast pyruvate decarboxylase of (a) pyruvate on a rapid-scan U

41 The E1 component (pyruvate decarboxylase) of the pyruvate dehydrogenase co

42 e measured, in microorganisms, the action of pyruvate decarboxylase (PDC) and pyruvate formate lyase

43 Benzoylformate decarboxylase (BFDC) and pyruvate decarboxylase (PDC) are both thiamin diphosphat

44 orylating; from Lactobacillus plantarum),and pyruvate decarboxylase (PDC) from Saccharomycescerevisia

45 Pyruvate decarboxylase (PDC) uses thiamine diphosphate a

46 ystem, based on alcohol dehydrogenase (ADH), pyruvate decarboxylase (PDC), and lactate dehydrogenase

47 d dual-processor ACs coencapsulating LOx and pyruvate decarboxylase (PDC), enabling selective convers

48 Plant pyruvate decarboxylases (PDC) catalyze the decarboxylati

49 olatile biosynthesis, and identified a melon pyruvate decarboxylase, PDC1, that is highly expressed i

50 of a prereaction intermediate of a bacterial pyruvate decarboxylase prepared by cocrystallizing the e

51 ecarboxylase, glyoxylate carboligase, indole pyruvate decarboxylase, pyruvate decarboxylase, the acet

52 and the Asp28-substituted variants of yeast pyruvate decarboxylase, suggesting that the active cente

53 carboligase, indole pyruvate decarboxylase, pyruvate decarboxylase, the acetyl phosphate-producing p

54 with the extensive genetic analysis of four pyruvate decarboxylases, the putative downstream compone

55 nds were then tested on three ThDP-dependent pyruvate decarboxylases: the Escherichia coli pyruvate d

56 hosphate organizes the active site pocket of pyruvate decarboxylase to support catalysis.

57 racemic LThDP was exposed to the E91D yeast pyruvate decarboxylase variant, or to the E1 subunit of

58 expression of hypoxic responsive genes (HRG) PYRUVATE DECARBOXYLASE (VvPDC), ALCOHOL DEHYDROGENASE (V

59 multienzyme complex that have evolved into a pyruvate decarboxylase, while other copies retained the

60 320-330 nm range, were investigated on yeast pyruvate decarboxylase (YPDC) and on the E1 subunit of t

61 A member of this superfamily, yeast pyruvate decarboxylase (YPDC) carries out the nonoxidati

62 The tetrameric enzyme yeast pyruvate decarboxylase (YPDC) has been known to dissocia

63 stal structure of pyruvamide-activated yeast pyruvate decarboxylase (YPDC) revealed a flexible loop s

64 Yeast pyruvate decarboxylase (YPDC), in addition to forming it

65 ted kinetic model for the mechanism of yeast pyruvate decarboxylase (YPDC, EC 4.1.1.1), an enzyme sub