Talk:V-ATPase

I have put this in Category:Transport proteins, but I'm not actually certain that they are transport proteins. Can someone confirm or confute? Thanks, delldot | talk 06:40, 9 January 2007 (UTC)Reply

Hi there! I'm actually reading about this in my biochemistry class right now, and yes, V-Type ATPases are transport proteins. However, I have some edits for the page. First, the first picture you put on (the one with the flower-shaped protein subunits) is not a V-type ATPase, but rather an F-type. I know it sounds pretty inconsequential, but the F-type ATPases are used as "energy-coupling factors" which generate ATP (in oxidative phosphorylation) whereas, like its said in this article, V-types are used to acidify intracellular compartments like the lysozome, Golgi body, etc. I'm not exactly that tech savvy, so I don't feel comfortable changing wikipedia, but perhaps if you get this, it might be done? Thanks so much :)

the reference I used for this is: Principles of Biochemistry; Lehninger, et al. 2008 5th Edition —Preceding unsigned comment added by 24.13.86.230 (talk) 05:04, 22 January 2009 (UTC)Reply

Can someone more in the know determine if "singe" = "single" ?Srednuas Lenoroc (talk) 11:57, 15 November 2015 (UTC)Reply

Once again, I'm sure it's "single", and that is confirmed by a Google search to be a term in use. JohnCD (talk) 12:21, 15 November 2015 (UTC)Reply

I am totally lost with sciences so would not know what was correct even if I did google it.Srednuas Lenoroc (talk) 12:27, 15 November 2015 (UTC)Reply

Roles played - In addition, other variety? of biological processes (varieties)

Disruption of the gene vma-1 gene - delete first gene

summary box - subunit C - crystal structure of subunit C (vma5p) of the yeast v-atpase - capitalize Crystal, Vma5p, & V-ATPase

Structure - The complex structure of the V-ATPase has been revealed through the structure of the M. Sexta and Yeast - don't capitalize sexta & yeast

summary box - subunit d/d2 - crystal structure of subunit C (yeast subunit d) of v-atpase - capitalize Crystal & V-ATPase and are termed Vma12p, Vma21p, and Vma22p.[12][13][14][15] - should [15] be [16]?

V1 - Unlike Vo, the V1 domain is hydrophobic?

summary box - subunit H, N-terminal - crystal structure of the regulatory subunit H of the v-type atpase of saccharomyces - capitalize Crystal, V-type, ATPase, & Saccharomyces

Subunit C V-ATPase (Vacuolar-ATPase) C represents the C terminal subunit that is part of the V1 complex - delete (Vacuolar-ATPase) & terminal; 1 should be a subscript

between the V1 and Vo complexes - 1 & o should be subscripts

Subunit C function - shouldn't this be combined with Subunit C?

catalytic (V1) and membrane (VO) sectors - should be 1 & o subscripts

dissociation of the V1 and Vo - should be 1 & o subscripts

Essentially, by creating a high electrochemical gradient and low pH, this powers the enzyme to create more ATP. - this sentence does not make sense; V-ATPase uses rather than produces ATP

Subunit H - free V1 subunits, it stops ATP hydrolysis when V1 and Vo - 1 & o should be subscripts

Vo - The Vo domain is hydrophilic?

Vo Subunits table - a/I is missing TCIRG1 (which encodes the a3 isoform)

Subunit a/I - in the Vo or Ao - o should be subscript

subunit a of FO - O should be subscript o

Subunit d/C - subunit C in A-ATpases, is a part of the Vo - capitalize P in A-ATPases & o in Vo should be subscript

V-ATPase assembly - The precise mechanisms by which V-ATPases assembly?

V-ATPase evolution - consisting of two different proteins evolves into the fungi version with three different proteins - change proteins to subunit c proteins

Regulation - by macrolide antibiotics, such as concanamycin (CCA) and balifomycin? (should be bafilomycin) - & add some before macrolide

Human diseases - Osteopetrosis - Osteopetrosis is generic name - add a before is

Mutations to the chloride channel ClC7 gene also lead to both dominant and recessive osteopetrosis.[40?]

References - 5 is wrong

External links - V-type+ATPase - should be V-Type ATPase

    108.18.223.247 (talk) 08:46, 19 November 2020 (UTC)Reply