ライフサイエンスコーパス: histidinol

1 on of l-histidinol 1-phosphate (HOLP) into l-histidinol.

2 th stereospecifically mono- and dideuterated histidinols.

3 tic pathway catalyzes dephosphorylation of l-histidinol 1-phosphate (HOLP) into l-histidinol.

4 namically unfavorable, hydride transfer from histidinol and a slower, irreversible second hydride tra

5 , L-histidinol phosphate, and a complex of L-histidinol and arsenate bound in the active site.

6 he hydrolysis of L-histidinol phosphate to L-histidinol and inorganic phosphate, the penultimate step

7 The ability to transport histidinol and other cations was conferred by single ami

8 n of HOL1, conferring the ability to take up histidinol; and (ii) cis-acting mutations (selected in a

9 ic fibroblasts survive under a wide range of histidinol-containing growth conditions and support grow

10 The dimeric zinc metalloenzyme L-histidinol dehydrogenase (HDH) catalyzes an unusual four

11 e last enzyme of the pathway, bifunctional L-histidinol dehydrogenase (HDH, EC 1.1.1.23), catalyses t

12 s conclusively that proteobacterial HisG and histidinol dehydrogenase (HisD) sequences are paraphylet

13 (THB1, GenBank accession no. AF023140), and histidinol dehydrogenase (THD1, GenBank accession no. AF

14 L-Histidinol dehydrogenase catalyzes the biosynthetic oxid

15 no acids within a nonconserved region of the histidinol dehydrogenase protein.

16 The hisD gene encodes the protein histidinol dehydrogenase, which catalyzes the conversion

17 ), catalyses two oxidation reactions: from L-histidinol (HOL) to L-histidinaldehyde and from L-histid

18 selection in cultures with media containing histidinol in place of histidine occurs by both histidin

19 unit, and 0.25 per subunit with dideuterated histidinol, indicating that the overall first half-react

20 Histidine limitation in the presence of histidinol induced a twofold increase in the phosphoryla

21 Histidinol is toxic to mammalian cells, while histidine

22 esults from kcat and kcat/KM titrations with histidinol, NAD, and the alternative substrate imidazoly

23 anti-mycobacterial drugs.The polymerase and histidinol phosphatase (PHP) domain in the DNA polymeras

24 HPP from the polymerase and histidinol phosphatase (PHP) family of proteins possesse

25 n, initially identified by its similarity to histidinol phosphatase but of otherwise unknown function

26 family, designated PHP, after polymerase and histidinol phosphatase.

27 is) = 60 microM, and K(ii) = 150 microM) and histidinol phosphate (K(is) = 1 mM, and K(ii) = 6 mM), w

28 ite are remarkably close to that observed in histidinol phosphate aminotransferase, which suggests th

29 a enterica, which is structurally similar to histidinol phosphate aminotransferase.

30 L-threonine-O-3-phosphate decarboxylase and histidinol phosphate aminotransferases, many of which ap

31 L-Histidinol phosphate phosphatase (HPP) catalyzes the hyd

32 iscovered in Arabidopsis thaliana plant-type histidinol phosphate phosphatase (HPP) shares no homolog

33 SynSerB3 up-regulates hisB, a gene encoding histidinol phosphate phosphatase.

34 sphatase (HPP) catalyzes the hydrolysis of L-histidinol phosphate to L-histidinol and inorganic phosp

35 tures of HPP were determined with sulfate, L-histidinol phosphate, and a complex of L-histidinol and

36 ated using hexose and heptose bisphosphates, histidinol phosphate, and common organophosphate metabol

37 sphate phosphatase (GmhB) is a member of the histidinol-phosphate phosphatase (HisB) subfamily of the

38 ish GmhB from its subfamily counterpart, the histidinol-phosphate phosphatase domain of HisB.

39 We show that GmhB and the histidinol-phosphate phosphatase domain use the same des

40 dine occurs by both histidine starvation and histidinol poisoning.

41 s, namely complexes with HOLP (substrate), l-histidinol (product), and PO4 (3-) (by-product) as well

42 ding for either neomycin-resistance (neo) or histidinol-resistance (hol), have been constructed for t

43 Stopped-flow experiments with protiated histidinol revealed a small burst of NADH production wit

44 To support ES cell stability under histidinol selection, mice transgenic for the S. typhimu

45 of Saccharomyces cerevisiae cells to take up histidinol, the biosynthetic precursor to histidine, res

46 se catalyzes the biosynthetic oxidation of L-histidinol to L-histidine with sequential reduction of t

47 drogenase, which catalyzes the conversion of histidinol to the amino acid histidine.

48 results had suggested that the oxidation of histidinol to the intermediate histidinaldehyde occurred

49 tion for spontaneous mutations that increase histidinol uptake by such HOL1 mutants resulted in mutat

50 four-electron oxidation of the amino alcohol histidinol via the histidinaldehyde intermediate to the