EC |
6.3.2.32 |
Accepted name: |
coenzyme γ-F420-2:α-L-glutamate ligase |
Reaction: |
ATP + coenzyme γ-F420-2 + L-glutamate = ADP + phosphate + coenzyme α-F420-3 |
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For diagram of coenzyme F420 biosynthesis, click here |
Other name(s): |
MJ1001; CofF protein; γ-F420-2:α-L-glutamate ligase |
Systematic name: |
L-glutamate:coenzyme γ-F420-2 (ADP-forming) |
Comments: |
The enzyme caps the γ-glutamyl tail of the hydride carrier coenzyme F420 [1]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Li, H., Xu, H., Graham, D.E. and White, R.H. Glutathione synthetase homologs encode α-L-glutamate ligases for methanogenic coenzyme F420 and tetrahydrosarcinapterin biosyntheses. Proc. Natl. Acad. Sci. USA 100 (2003) 9785–9790. [DOI] [PMID: 12909715] |
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[EC 6.3.2.32 created 2010] |
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EC |
6.3.2.33 |
Accepted name: |
tetrahydrosarcinapterin synthase |
Reaction: |
ATP + tetrahydromethanopterin + L-glutamate = ADP + phosphate + 5,6,7,8-tetrahydrosarcinapterin |
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For diagram of methanopterin biosynthesis (part 4), click here |
Other name(s): |
H4MPT:α-L-glutamate ligase; MJ0620; MptN protein |
Systematic name: |
tetrahydromethanopterin:α-L-glutamate ligase (ADP-forming) |
Comments: |
This enzyme catalyses the biosynthesis of 5,6,7,8-tetrahydrosarcinapterin, a modified form of tetrahydromethanopterin found in the Methanosarcinales. It does not require K+, and does not discriminate between ATP and GTP [1]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Li, H., Xu, H., Graham, D.E. and White, R.H. Glutathione synthetase homologs encode α-L-glutamate ligases for methanogenic coenzyme F420 and tetrahydrosarcinapterin biosyntheses. Proc. Natl. Acad. Sci. USA 100 (2003) 9785–9790. [DOI] [PMID: 12909715] |
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[EC 6.3.2.33 created 2010] |
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EC |
7.1.1.1 |
Accepted name: |
proton-translocating NAD(P)+ transhydrogenase |
Reaction: |
NADPH + NAD+ + H+[side 1] = NADP+ + NADH + H+[side 2] |
Other name(s): |
pntA (gene name); pntB (gene name); NNT (gene name) |
Systematic name: |
NADPH:NAD+ oxidoreductase (H+-transporting) |
Comments: |
The enzyme is a membrane bound proton-translocating pyridine nucleotide transhydrogenase that couples the reversible reduction of NADP by NADH to an inward proton translocation across the membrane. In the bacterium Escherichia coli the enzyme provides a major source of cytosolic NADPH. Detoxification of reactive oxygen species in mitochondria by glutathione peroxidases depends on NADPH produced by this enzyme. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Clarke, D.M. and Bragg, P.D. Cloning and expression of the transhydrogenase gene of Escherichia coli. J. Bacteriol. 162 (1985) 367–373. [DOI] [PMID: 3884596] |
2. |
Clarke, D.M. and Bragg, P.D. Purification and properties of reconstitutively active nicotinamide nucleotide transhydrogenase of Escherichia coli. Eur. J. Biochem. 149 (1985) 517–523. [DOI] [PMID: 3891338] |
3. |
Glavas, N.A., Hou, C. and Bragg, P.D. Involvement of histidine-91 of the β subunit in proton translocation by the pyridine nucleotide transhydrogenase of Escherichia coli. Biochemistry 34 (1995) 7694–7702. [DOI] [PMID: 7779816] |
4. |
Sauer, U., Canonaco, F., Heri, S., Perrenoud, A. and Fischer, E. The soluble and membrane-bound transhydrogenases UdhA and PntAB have divergent functions in NADPH metabolism of Escherichia coli. J. Biol. Chem. 279 (2004) 6613–6619. [DOI] [PMID: 14660605] |
5. |
Bizouarn, T., Fjellstrom, O., Meuller, J., Axelsson, M., Bergkvist, A., Johansson, C., Goran Karlsson, B. and Rydstrom, J. Proton translocating nicotinamide nucleotide transhydrogenase from E. coli. Mechanism of action deduced from its structural and catalytic properties. Biochim. Biophys. Acta 1457 (2000) 211–228. [DOI] [PMID: 10773166] |
6. |
White, S.A., Peake, S.J., McSweeney, S., Leonard, G., Cotton, N.P. and Jackson, J.B. The high-resolution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from human heart mitochondria. Structure 8 (2000) 1–12. [DOI] [PMID: 10673423] |
7. |
Johansson, T., Oswald, C., Pedersen, A., Tornroth, S., Okvist, M., Karlsson, B.G., Rydstrom, J. and Krengel, U. X-ray structure of domain I of the proton-pumping membrane protein transhydrogenase from Escherichia coli. J. Mol. Biol. 352 (2005) 299–312. [DOI] [PMID: 16083909] |
8. |
Meimaridou, E., Kowalczyk, J., Guasti, L., Hughes, C.R., Wagner, F., Frommolt, P., Nurnberg, P., Mann, N.P., Banerjee, R., Saka, H.N., Chapple, J.P., King, P.J., Clark, A.J. and Metherell, L.A. Mutations in NNT encoding nicotinamide nucleotide transhydrogenase cause familial glucocorticoid deficiency. Nat. Genet. 44 (2012) 740–742. [DOI] [PMID: 22634753] |
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[EC 7.1.1.1 created 2015 as EC 1.6.1.5, transferred 2018 to EC 7.1.1.1 (EC 1.6.1.2 created 1986, incorporated 2023)] |
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EC |
7.2.2.2 |
Accepted name: |
ABC-type Cd2+ transporter |
Reaction: |
ATP + H2O + Cd2+[side 1] = ADP + phosphate + Cd2+[side 2] |
Other name(s): |
cadmium-transporting ATPase (ambiguous); ABC-type cadmium-transporter |
Systematic name: |
ATP phosphohydrolase (ABC-type, heavy-metal-exporting) |
Comments: |
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. A yeast enzyme that exports some heavy metals, especially Cd2+, from the cytosol into the vacuole. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Li, Z.S., Szczypka, M., Lu, Y.P., Thiele, D.J. and Rea, P.A. The yeast cadmium factor protein (YCF1) is a vacuolar glutathione S-conjugate pump. J. Biol. Chem. 271 (1996) 6509–6517. [DOI] [PMID: 8626454] |
2. |
Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81–136. [PMID: 9889977] |
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[EC 7.2.2.2 created 2000 as EC 3.6.3.46, transferred 2018 to EC 7.2.2.2] |
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EC |
7.4.2.10 |
Accepted name: |
ABC-type glutathione transporter |
Reaction: |
ATP + H2O + glutathione-[glutathione-binding protein][side 1] = ADP + phosphate + glutathione[side 2] + [glutathione-binding protein][side 1] |
Other name(s): |
glutathione transporting ATPase; glutathione ABC transporter; gsiACD (gene names) |
Systematic name: |
ATP phosphohydrolase (ABC-type,glutathione-importing) |
Comments: |
A prokaryotic ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme from the bacterium Escherichia coli is a heterotrimeric complex that interacts with an extracytoplasmic substrate binding protein to mediate the uptake of glutathione. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Suzuki, H., Koyanagi, T., Izuka, S., Onishi, A. and Kumagai, H. The yliA, -B, -C, and -D genes of Escherichia coli K-12 encode a novel glutathione importer with an ATP-binding cassette. J. Bacteriol. 187 (2005) 5861–5867. [PMID: 16109926] |
2. |
Moussatova, A., Kandt, C., O'Mara, M.L. and Tieleman, D.P. ATP-binding cassette transporters in Escherichia coli. Biochim. Biophys. Acta 1778 (2008) 1757–1771. [PMID: 18634750] |
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[EC 7.4.2.10 created 2019] |
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EC |
7.6.2.2 |
Accepted name: |
ABC-type xenobiotic transporter |
Reaction: |
ATP + H2O + xenobiotic[side 1] = ADP + phosphate + xenobiotic[side 2] |
Other name(s): |
xenobiotic-transporting ATPase; multidrug-resistance protein; MDR protein; P-glycoprotein; pleiotropic-drug-resistance protein; PDR protein; steroid-transporting ATPase; ATP phosphohydrolase (steroid-exporting) |
Systematic name: |
ATP phosphohydrolase (ABC-type, xenobiotic-exporting) |
Comments: |
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. The enzymes from Gram-positive bacteria and eukaryotic cells export a number of drugs with unusual specificity, covering various groups of unrelated substances while ignoring some that are closely related structurally. Several distinct enzymes may be present in a single eukaryotic cell. Many of them also transport glutathione—drug conjugates (see EC 7.6.2.3, ABC-type glutathione-S-conjugate transporter) while others also show some ’flippase’ activity (cf. EC 7.6.2.1, P-type phospholipid transporter). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Bellamy, W.T. P-glycoproteins and multidrug resistance. Annu. Rev. Pharmacol. Toxicol. 36 (1996) 161–183. [DOI] [PMID: 8725386] |
2. |
Frijters, C.M., Ottenhoff, R., Van Wijland, M.J., Van Nieuwkerk, C., Groen, A.K. and Oude-Elferink, R.P. Influence of bile salts on hepatic mdr2 P-glycoprotein expression. Adv. Enzyme Regul. 36 (1996) 351–363. [DOI] [PMID: 8869755] |
3. |
Keppler, D., König, J. and Buchler, M. The canalicular multidrug resistance protein, cMRP/MRP2, a novel conjugate export pump expressed in the apical membrane of hepatocytes. Adv. Enzyme Regul. 37 (1997) 321–333. [DOI] [PMID: 9381978] |
4. |
Loe, D.W., Deeley, R.G. and Cole, S.P. Characterization of vincristine transport by the Mr 190,000 multidrug resistance protein (MRP): evidence for cotransport with reduced glutathione. Cancer Res. 58 (1998) 5130–5136. [PMID: 9823323] |
5. |
van Veen, H.W. and Konings, W.N. The ABC family of multidrug transporters in microorganisms. Biochim. Biophys. Acta 1365 (1998) 31–36. [DOI] [PMID: 9693718] |
6. |
Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998. |
7. |
Prasad, R., De Wergifosse, P., Goffeau, A. and Balzi, E. Molecular cloning and characterization of a novel gene of Candida albicans, CDR1, conferring multiple resistance to drugs and antifungals. Curr. Genet. 27 (1995) 320–329. [PMID: 7614555] |
8. |
Nagao, K., Taguchi, Y., Arioka, M., Kadokura, H., Takatsuki, A., Yoda, K. and Yamasaki, M. bfr1+, a novel gene of Schizosaccharomyces pombe which confers brefeldin A resistance, is structurally related to the ATP-binding cassette superfamily. J. Bacteriol. 177 (1995) 1536–1543. [DOI] [PMID: 7883711] |
9. |
Mahé, Y., Lemoine, Y. and Kuchler, K. The ATP-binding cassette transporters Pdr5 and Snq2 of Saccharomyces cerevisiae can mediate transport of steroids in vivo. J. Biol. Chem. 271 (1996) 25167–25172. [DOI] [PMID: 8810273] |
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[EC 7.6.2.2 created 2000 as EC 3.6.3.44 (EC 3.6.3.45 incorporated 2006), modified 2006, transferred 2018 to EC 7.6.2.2] |
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EC |
7.6.2.3 |
Accepted name: |
ABC-type glutathione-S-conjugate transporter |
Reaction: |
ATP + H2O + glutathione-S-conjugate[side 1] = ADP + phosphate + glutathione-S-conjugate[side 2] |
Other name(s): |
multidrug resistance-associated protein 1; glutathione-S-conjugate-translocating ATPase; MRP; MRP1; ABCC1 (gene name); YBT1 (gene name); YCF1 (gene name) |
Systematic name: |
ATP phosphohydrolase (ABC-type, glutathione-S-conjugate-exporting) |
Comments: |
A eukaryotic ATP-binding cassette (ABC) type transporter that mediates the transport of glutathione-S-conjugates. The mammalian enzyme, which also transports some glucuronides, exports the substrates out of the cell, while plant and fungal transporters export them into the vacuole. Over-expression confers resistance to anticancer drugs by their efficient exportation in glutathione-S-conjugate form. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Zaman, G.J., Flens, M.J., van Leusden, M.R., de Haas, M., Mulder, H.S., Lankelma, J., Pinedo, H.M., Scheper, R.J., Baas, F., Broxterman, H.J. and et al. The human multidrug resistance-associated protein MRP is a plasma membrane drug-efflux pump. Proc. Natl. Acad. Sci. USA 91 (1994) 8822–8826. [PMID: 7916458] |
2. |
Lautier, D., Canitrot, Y., Deeley, R.G. and Cole, S.P. Multidrug resistance mediated by the multidrug resistance protein (MRP) gene. Biochem. Pharmacol. 52 (1996) 967–977. [PMID: 8831715] |
3. |
Li, Z.S., Szczypka, M., Lu, Y.P., Thiele, D.J. and Rea, P.A. The yeast cadmium factor protein (YCF1) is a vacuolar glutathione S-conjugate pump. J. Biol. Chem. 271 (1996) 6509–6517. [DOI] [PMID: 8626454] |
4. |
Lu, Y.P., Li, Z.S. and Rea, P.A. AtMRP1 gene of Arabidopsis encodes a glutathione S-conjugate pump: isolation and functional definition of a plant ATP-binding cassette transporter gene. Proc. Natl. Acad. Sci. USA 94 (1997) 8243–8248. [PMID: 9223346] |
5. |
Cole, S.P. Multidrug resistance protein 1 (MRP1, ABCC1), a "multitasking" ATP-binding cassette (ABC) transporter. J. Biol. Chem. 289 (2014) 30880–30888. [PMID: 25281745] |
6. |
Cordente, A.G., Capone, D.L. and Curtin, C.D. Unravelling glutathione conjugate catabolism in Saccharomyces cerevisiae: the role of glutathione/dipeptide transporters and vacuolar function in the release of volatile sulfur compounds 3-mercaptohexan-1-ol and 4-mercapto-4-methylpentan-2-one. Appl. Microbiol. Biotechnol. 99 (2015) 9709–9722. [PMID: 26227410] |
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[EC 7.6.2.3 created 2018] |
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