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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 midazole alkaloids derived from histamine or histidinol and generally investigating the occurrence of
7 he hydrolysis of L-histidinol phosphate to L-histidinol and inorganic phosphate, the penultimate step
8                     The ability to transport histidinol and other cations was conferred by single ami
9 n of HOL1, conferring the ability to take up histidinol; and (ii) cis-acting mutations (selected in a
10 ic fibroblasts survive under a wide range of histidinol-containing growth conditions and support grow
11             The dimeric zinc metalloenzyme L-histidinol dehydrogenase (HDH) catalyzes an unusual four
12 e last enzyme of the pathway, bifunctional L-histidinol dehydrogenase (HDH, EC 1.1.1.23), catalyses t
13 s conclusively that proteobacterial HisG and histidinol dehydrogenase (HisD) sequences are paraphylet
14  (THB1, GenBank accession no. AF023140), and histidinol dehydrogenase (THD1, GenBank accession no. AF
15                                            L-Histidinol dehydrogenase catalyzes the biosynthetic oxid
16 no acids within a nonconserved region of the histidinol dehydrogenase protein.
17            The hisD gene encodes the protein histidinol dehydrogenase, which catalyzes the conversion
18 ), catalyses two oxidation reactions: from L-histidinol (HOL) to L-histidinaldehyde and from L-histid
19  selection in cultures with media containing histidinol in place of histidine occurs by both histidin
20 unit, and 0.25 per subunit with dideuterated histidinol, indicating that the overall first half-react
21      Histidine limitation in the presence of histidinol induced a twofold increase in the phosphoryla
22                                              Histidinol is toxic to mammalian cells, while histidine
23 esults from kcat and kcat/KM titrations with histidinol, NAD, and the alternative substrate imidazoly
24  anti-mycobacterial drugs.The polymerase and histidinol phosphatase (PHP) domain in the DNA polymeras
25                  HPP from the polymerase and histidinol phosphatase (PHP) family of proteins possesse
26 n, initially identified by its similarity to histidinol phosphatase but of otherwise unknown function
27 oenzymes that are part of the polymerase and histidinol phosphatase superfamily.
28 family, designated PHP, after polymerase and histidinol phosphatase.
29 member of a previously unrecognised class of histidinol-phosphatases; a set of 20 genes required for
30 is) = 60 microM, and K(ii) = 150 microM) and histidinol phosphate (K(is) = 1 mM, and K(ii) = 6 mM), w
31 ite are remarkably close to that observed in histidinol phosphate aminotransferase, which suggests th
32 a enterica, which is structurally similar to histidinol phosphate aminotransferase.
33  L-threonine-O-3-phosphate decarboxylase and histidinol phosphate aminotransferases, many of which ap
34                                            L-Histidinol phosphate phosphatase (HPP) catalyzes the hyd
35 iscovered in Arabidopsis thaliana plant-type histidinol phosphate phosphatase (HPP) shares no homolog
36  SynSerB3 up-regulates hisB, a gene encoding histidinol phosphate phosphatase.
37 sphatase (HPP) catalyzes the hydrolysis of L-histidinol phosphate to L-histidinol and inorganic phosp
38 tures of HPP were determined with sulfate, L-histidinol phosphate, and a complex of L-histidinol and
39 ated using hexose and heptose bisphosphates, histidinol phosphate, and common organophosphate metabol
40 sphate phosphatase (GmhB) is a member of the histidinol-phosphate phosphatase (HisB) subfamily of the
41 ish GmhB from its subfamily counterpart, the histidinol-phosphate phosphatase domain of HisB.
42                    We show that GmhB and the histidinol-phosphate phosphatase domain use the same des
43 dine occurs by both histidine starvation and histidinol poisoning.
44 s, namely complexes with HOLP (substrate), l-histidinol (product), and PO4 (3-) (by-product) as well
45 ding for either neomycin-resistance (neo) or histidinol-resistance (hol), have been constructed for t
46      Stopped-flow experiments with protiated histidinol revealed a small burst of NADH production wit
47           To support ES cell stability under histidinol selection, mice transgenic for the S. typhimu
48 of Saccharomyces cerevisiae cells to take up histidinol, the biosynthetic precursor to histidine, res
49 se catalyzes the biosynthetic oxidation of L-histidinol to L-histidine with sequential reduction of t
50 drogenase, which catalyzes the conversion of histidinol to the amino acid histidine.
51  results had suggested that the oxidation of histidinol to the intermediate histidinaldehyde occurred
52 tion for spontaneous mutations that increase histidinol uptake by such HOL1 mutants resulted in mutat
53 four-electron oxidation of the amino alcohol histidinol via the histidinaldehyde intermediate to the