Search results
From Proteopedia
You searched for Molybdoenzyme
There is no page with the exact title "Molybdoenzyme". The search results for "Molybdoenzyme" are displayed below. You can create a page titled Molybdoenzyme (by clicking on the red link).
For more information about searching Proteopedia, see Help.
Showing below up to 20 results starting with #1.
View (previous 20) (next 20) (20 | 50 | 100 | 250 | 500)
Article title matches
- Category:Molybdoenzyme (44 bytes)
1: List of pages with the keyword Molybdoenzyme
Page text matches
- 1e5k (5,482 bytes)
11: ...fficient for the in vitro activation of the DMSOR molybdoenzyme that uses the Mo-bisMGD form of molybdenum cofact...
24: ...is required for the functioning of many bacterial molybdoenzymes, including the nitrate reductases, dimethylsulfo... - 1e18 (4,116 bytes)
24: ...m Rhodobacter capsulatus, well-characterised as a molybdoenzyme, will bind tungsten. Protein crystallography has ... - 1hjl (5,131 bytes)
11: ...fficient for the in vitro activation of the DMSOR molybdoenzyme that uses the Mo-bisMGD form of molybdenum cofact...
24: ...at is required for the activity of most bacterial molybdoenzymes. MGD is synthesized from molybdopterin (MPT) and... - 1hjj (5,134 bytes)
11: ...fficient for the in vitro activation of the DMSOR molybdoenzyme that uses the Mo-bisMGD form of molybdenum cofact...
24: ...at is required for the activity of most bacterial molybdoenzymes. MGD is synthesized from molybdopterin (MPT) and... - 1h4d (5,134 bytes)
11: ...fficient for the in vitro activation of the DMSOR molybdoenzyme that uses the Mo-bisMGD form of molybdenum cofact...
24: ...at is required for the activity of most bacterial molybdoenzymes. MGD is synthesized from molybdopterin (MPT) and... - 1h4e (5,134 bytes)
11: ...fficient for the in vitro activation of the DMSOR molybdoenzyme that uses the Mo-bisMGD form of molybdenum cofact...
24: ...at is required for the activity of most bacterial molybdoenzymes. MGD is synthesized from molybdopterin (MPT) and... - 1h4c (5,134 bytes)
11: ...fficient for the in vitro activation of the DMSOR molybdoenzyme that uses the Mo-bisMGD form of molybdenum cofact...
24: ...at is required for the activity of most bacterial molybdoenzymes. MGD is synthesized from molybdopterin (MPT) and... - 1jlj (5,894 bytes)
11: ...isease which leads to the pleiotropic loss of all molybdoenzyme activities and is characterized by severe neurolo... - 1fr9 (3,235 bytes)
11: ...fficient for the in vitro activation of the DMSOR molybdoenzyme that uses the Mo-bisMGD form of molybdenum cofact... - 1frw (3,388 bytes)
11: ...fficient for the in vitro activation of the DMSOR molybdoenzyme that uses the Mo-bisMGD form of molybdenum cofact... - 1n1c (4,131 bytes)
24: ...asmic chaperone involved in the maturation of the molybdoenzyme TorA prior to the translocation of the folded pro... - 1xdy (5,872 bytes)
24: ...additional nucleotide, and it represents the only molybdoenzyme isolated from E. coli characterized by the presen... - 1b25 (4,385 bytes)
24: ...ive site structures between FOR and the unrelated molybdoenzyme aldehyde oxidoreductase from Desulfovibrio gigas ... - 1b4n (4,525 bytes)
24: ...ive site structures between FOR and the unrelated molybdoenzyme aldehyde oxidoreductase from Desulfovibrio gigas ... - Category:Molybdoenzyme (44 bytes)
1: List of pages with the keyword Molybdoenzyme - 3hrd (4,537 bytes)
24: ...dehydrogenase (NDH) from Eubacterium barkeri is a molybdoenzyme catalyzing the hydroxylation of nicotinate to 6-h... - ModG (6,247 bytes)
6: ...4640</ref> It is also part of the cofactor of the molybdoenzyme ModG. Not surprisingly, studies have linked ModG ...
10: The molybdoenzyme is a homotrimer.<ref name="MODGR1"/> It can bind ... - 4ap8 (2,712 bytes)
11: ...isease which leads to the pleiotropic loss of all molybdoenzyme activities and is characterized by severe neurolo... - 6btm (4,269 bytes)
14: ... homologous to members of the complex iron-sulfur molybdoenzyme (CISM) superfamily (8) , including the proton pum...
View (previous 20) (next 20) (20 | 50 | 100 | 250 | 500)
