|
|
| Line 1: |
Line 1: |
| {{enzyme
| | Hi there, I am Andrew Berryhill. Ohio is exactly where his house is and his family enjoys it. She functions as a travel agent but soon she'll be on her own. The favorite hobby for him and his kids is style and he'll be beginning something else alongside with it.<br><br>Check out my web-site ... [http://1.234.36.240/fxac/m001_2/7330 psychic phone] |
| | Name = histidinol dehydrogenase
| |
| | EC_number = 1.1.1.23
| |
| | CAS_number = 9028-27-7
| |
| | IUBMB_EC_number = 1/1/1/23
| |
| | GO_code = 0004399
| |
| | image =
| |
| | width =
| |
| | caption =
| |
| }}
| |
| {{Infobox protein family
| |
| | Symbol = Histidinol_dh
| |
| | Name = Histidinol dehydrogenase
| |
| | image = PDB 1k75 EBI.jpg
| |
| | width =
| |
| | caption = the l-histidinol dehydrogenase (hisd) structure implicates domain swapping and gene duplication.
| |
| | Pfam = PF00815
| |
| | Pfam_clan = CL0099
| |
| | InterPro = IPR012131
| |
| | SMART =
| |
| | PROSITE = PDOC00534
| |
| | MEROPS =
| |
| | SCOP = 1k75
| |
| | TCDB =
| |
| | OPM family =
| |
| | OPM protein =
| |
| | CAZy =
| |
| | CDD =
| |
| }}
| |
| In [[enzymology]], a '''histidinol dehydrogenase''' (HIS4) (HDH) ({{EC number|1.1.1.23}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]
| |
| | |
| :L-histidinol + 2 NAD<sup>+</sup> <math>\rightleftharpoons</math> L-histidine + 2 NADH + 2 H<sup>+</sup>
| |
| | |
| Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[L-histidinol]] and [[nicotinamide adenine dinucleotide|NAD<sup>+</sup>]], whereas its 3 [[product (chemistry)|products]] are [[L-histidine]], [[nicotinamide adenine dinucleotide|NADH]], and [[hydrogen ion|H<sup>+</sup>]].
| |
| | |
| This enzyme belongs to the family of [[oxidoreductase]]s, specifically those acting on the CH-OH group of donor with NAD<sup>+</sup> or NADP<sup>+</sup> as acceptor. The systematic name of this enzyme class is '''L-histidinol:NAD<sup>+</sup> oxidoreductase'''. This enzyme is also called '''L-histidinol dehydrogenase'''.
| |
| | |
| Histidinol dehydrogenase [[Catalysis|catalyzes]] the terminal step in the [[biosynthesis]] of [[histidine]] in [[bacteria]], [[fungi]], and [[plants]], the four-[[electron]] [[redox|oxidation]] of L-histidinol to histidine.
| |
| | |
| In 4-electron dehydrogenases, a single [[active site]] [[catalysis|catalyses]] 2 separate [[oxidation]] steps: oxidation of the [[Enzyme substrate|substrate]] [[alcohol]] to an [[reaction intermediate|intermediate]] [[aldehyde]]; and oxidation of the aldehyde to the [[product (chemistry)|product]] acid, in this case His.<ref name="pmid3533140">{{cite journal | author = Grubmeyer CT, Gray WR | title = A cysteine residue (cysteine-116) in the histidinol binding site of histidinol dehydrogenase | journal = Biochemistry | volume = 25 | issue = 17 | pages = 4778–84 |date=August 1986 | pmid = 3533140 | doi = 10.1021/bi00365a009| url = }}</ref> The reaction proceeds via a tightly- or covalently-bound inter-mediate, and requires the presence of 2 NAD [[molecule]]s.<ref name="pmid3533140">{{cite journal | author = Grubmeyer CT, Gray WR | title = A cysteine residue (cysteine-116) in the histidinol binding site of histidinol dehydrogenase | journal = Biochemistry | volume = 25 | issue = 17 | pages = 4778–84 |date=August 1986 | pmid = 3533140 | doi = 10.1021/bi00365a009| url = }}</ref> By contrast with most [[dehydrogenases]], the [[Substrate (biochemistry)|substrate]] is bound before the [[Nicotinamide adenine dinucleotide|NAD]] [[coenzyme]].<ref name="pmid3533140">{{cite journal | author = Grubmeyer CT, Gray WR | title = A cysteine residue (cysteine-116) in the histidinol binding site of histidinol dehydrogenase | journal = Biochemistry | volume = 25 | issue = 17 | pages = 4778–84 |date=August 1986 | pmid = 3533140 | doi = 10.1021/bi00365a009| url = }}</ref> A [[Cysteine|Cys]] residue has been implicated in the catalytic mechanism of the second oxidative step.<ref name="pmid3533140">{{cite journal | author = Grubmeyer CT, Gray WR | title = A cysteine residue (cysteine-116) in the histidinol binding site of histidinol dehydrogenase | journal = Biochemistry | volume = 25 | issue = 17 | pages = 4778–84 |date=August 1986 | pmid = 3533140 | doi = 10.1021/bi00365a009| url = }}</ref>
| |
| | |
| In bacteria HDH is a single chain polypeptide; in [[fungus|fungi]] it is the C-terminal [[protein domain|domain]] of a multifunctional [[enzyme]] which [[catalyse]]s three different steps of histidine biosynthesis; and in [[plants]] it is [[gene expression|expressed]] as a [[cell nucleus|nuclear]] encoded [[protein]] [[Protein precursor|precursor]] which is exported to the [[chloroplast]].<ref name="pmid2034659">{{cite journal | author = Nagai A, Ward E, Beck J, Tada S, Chang JY, Scheidegger A, Ryals J | title = Structural and functional conservation of histidinol dehydrogenase between plants and microbes | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 88 | issue = 10 | pages = 4133–7 |date=May 1991 | pmid = 2034659 | pmc = 51612 | doi = 10.1073/pnas.88.10.4133| url = }}</ref><ref name="pmid15299582">{{cite journal | author = Cowan-Jacob SW, Rahuel J, Nagai A, Iwasaki G, Ohta D | title = Crystallization and preliminary crystallographic analysis of cabbage histidinol dehydrogenase | journal = Acta Crystallogr. D Biol. Crystallogr. | volume = 52 | issue = Pt 6 | pages = 1188–90 |date=November 1996 | pmid = 15299582 | doi = 10.1107/S0907444996008396 | url = }}</ref><ref name="pmid11842181">{{cite journal | author = Barbosa JA, Sivaraman J, Li Y, Larocque R, Matte A, Schrag JD, Cygler M | title = Mechanism of action and NAD<sup>+</sup>-binding mode revealed by the crystal structure of L-histidinol dehydrogenase | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 99 | issue = 4 | pages = 1859–64 |date=February 2002 | pmid = 11842181 | pmc = 122284 | doi = 10.1073/pnas.022476199 | url = }}</ref>
| |
| | |
| ==Structural studies==
| |
| | |
| As of late 2007, 4 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|1K75}}, {{PDB link|1KAE}}, {{PDB link|1KAH}}, and {{PDB link|1KAR}}.
| |
| | |
| ==References==
| |
| {{reflist|1}}
| |
| | |
| ==Further reading==
| |
| * {{cite journal | author = Adams E | year = 1954 | title = Enzymatic synthesis of histidine from histidinol | journal = J. Biol. Chem. | volume = 209 | pages = 829–846 | pmid=13192138 | issue = 2}}
| |
| * {{cite journal | author = Adams E | year = 1955 | title = L-Histidinal, a biosynthetic precursor of histidine | journal = J. Biol. Chem. | volume = 217 | pages = 325–344 | pmid=13271397 | issue = 1}}
| |
| * {{cite journal | author = Yourno J, Ino I | year = 1968 | title = Purification and crystallization of histidinol dehydrogenase from ''Salmonella typhimurium'' LT-2 | journal = J. Biol. Chem. | volume = 243 | pages = 3273–6 | pmid = 4872177 | issue = 12 }}
| |
| * {{cite journal | author = Loper JC | year = 1968 | title = Histidinol dehydrogenase from ''Salmonella typhimurium'' Crystallization and composition studies | journal = J. Biol. Chem. | volume = 243 | pages = 3264–72 | pmid = 4872176 | issue = 12 }}
| |
| | |
| {{InterPro content|IPR012131}}
| |
| | |
| [[Category:Protein families]]
| |
| [[Category:EC 1.1.1]]
| |
| [[Category:NADH-dependent enzymes]]
| |
| [[Category:Enzymes of known structure]]
| |
| | |
| {{1.1.1-enzyme-stub}}
| |
Hi there, I am Andrew Berryhill. Ohio is exactly where his house is and his family enjoys it. She functions as a travel agent but soon she'll be on her own. The favorite hobby for him and his kids is style and he'll be beginning something else alongside with it.
Check out my web-site ... psychic phone