The Enzyme Database

Your query returned 9 entries.    printer_iconPrintable version

EC 1.1.1.210     
Accepted name: 3β(or 20α)-hydroxysteroid dehydrogenase
Reaction: 5α-androstan-3β,17β-diol + NADP+ = 17β-hydroxy-5α-androstan-3-one + NADPH + H+
Other name(s): progesterone reductase; dehydrogenase, 3β,20α-hydroxy steroid; 3β,20α-hydroxysteroid oxidoreductase
Systematic name: 3β(or 20α)-hydroxysteroid:NADP+ oxidoreductase
Comments: Also acts on 20α-hydroxysteroids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 82869-26-9
References:
1.  Sharaf, M.A. and Sweet, F. Dual activity at an enzyme active site: 3β,20α-hydroxysteroid oxidoreductase from fetal blood. Biochemistry 21 (1982) 4615–4620. [PMID: 6958329]
[EC 1.1.1.210 created 1986]
 
 
EC 1.1.2.10     
Accepted name: lanthanide-dependent methanol dehydrogenase
Reaction: methanol + 2 oxidized cytochrome cL = formaldehyde + 2 reduced cytochrome cL
Other name(s): XoxF; XoxF-MDH; Ce-MDH; La3+-dependent MDH; Ce3+-induced methanol dehydrogenase; cerium dependent MDH
Systematic name: methanol:cytochrome cL oxidoreductase
Comments: Isolated from the bacterium Methylacidiphilum fumariolicum and many Methylobacterium species. Requires La3+, Ce3+, Pr3+ or Nd3+. The higher lanthanides show decreasing activity with Sm3+, Eu3+ and Gd3+. The lanthanide is coordinated by the enzyme and pyrroloquinoline quinone. Shows little activity with Ca2+, the required cofactor of EC 1.1.2.7, methanol dehydrogenase (cytochrome c).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hibi, Y., Asai, K., Arafuka, H., Hamajima, M., Iwama, T. and Kawai, K. Molecular structure of La3+-induced methanol dehydrogenase-like protein in Methylobacterium radiotolerans. J. Biosci. Bioeng. 111 (2011) 547–549. [PMID: 21256798]
2.  Nakagawa, T., Mitsui, R., Tani, A., Sasa, K., Tashiro, S., Iwama, T., Hayakawa, T. and Kawai, K. A catalytic role of XoxF1 as La3+-dependent methanol dehydrogenase in Methylobacterium extorquens strain AM1. PLoS One 7:e50480 (2012). [PMID: 23209751]
3.  Pol, A., Barends, T.R., Dietl, A., Khadem, A.F., Eygensteyn, J., Jetten, M.S. and Op den Camp, H.J. Rare earth metals are essential for methanotrophic life in volcanic mudpots. Environ. Microbiol. 16 (2014) 255–264. [PMID: 24034209]
4.  Bogart, J.A., Lewis, A.J. and Schelter, E.J. DFT study of the active site of the XoxF-type natural, cerium-dependent methanol dehydrogenase enzyme. Chemistry Eur. J. 21 (2015) 1743–1748. [PMID: 25421364]
5.  Prejano, M., Marino, T. and Russo, N. How can methanol dehydrogenase from Methylacidiphilum fumariolicum work with the alien Ce(III) ion in the active center? A theoretical study. Chemistry 23 (2017) 8652–8657. [PMID: 28488399]
6.  Masuda, S., Suzuki, Y., Fujitani, Y., Mitsui, R., Nakagawa, T., Shintani, M. and Tani, A. Lanthanide-dependent regulation of methylotrophy in Methylobacterium aquaticum strain 22A. mSphere 3 (2018) e00462. [PMID: 29404411]
[EC 1.1.2.10 created 2019]
 
 
EC 3.1.26.13     
Accepted name: retroviral ribonuclease H
Reaction: Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA [1-4]. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction [5]. 2. RNA 5′-end directed cleavage 13-19 nucleotides from the RNA end [6,7]. 3. DNA 3′-end directed cleavage 15-20 nucleotides away from the primer terminus [8-10].
Other name(s): RT/RNase H; retroviral reverse transcriptase RNaseH (gene name); HIV RNase H
Comments: Retroviral reverse transcriptase is a multifunctional enzyme responsible for viral replication. To perform this task the enzyme combines two distinct activities. The polymerase domain (EC 2.7.7.49, RNA-directed DNA polymerase) occupies the N-terminal two-thirds of the reverse transcriptase whereas the ribonuclease H domain comprises the C-terminal remaining one-third [13,14]. The RNase H domains of Moloney murine leukemia virus and Human immunodeficiency virus display two metal binding sites [15-17]
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9050-76-4
References:
1.  Schultz, S.J., Zhang, M. and Champoux, J.J. Recognition of internal cleavage sites by retroviral RNases H. J. Mol. Biol. 344 (2004) 635–652. [DOI] [PMID: 15533434]
2.  Sarafianos, S.G., Das, K., Tantillo, C., Clark, A.D., Jr., Ding, J., Whitcomb, J.M., Boyer, P.L., Hughes, S.H. and Arnold, E. Crystal structure of HIV-1 reverse transcriptase in complex with a polypurine tract RNA:DNA. EMBO J. 20 (2001) 1449–1461. [DOI] [PMID: 11250910]
3.  Rausch, J.W., Lener, D., Miller, J.T., Julias, J.G., Hughes, S.H. and Le Grice, S.F. Altering the RNase H primer grip of human immunodeficiency virus reverse transcriptase modifies cleavage specificity. Biochemistry 41 (2002) 4856–4865. [DOI] [PMID: 11939780]
4.  Brehm, J.H., Mellors, J.W. and Sluis-Cremer, N. Mechanism by which a glutamine to leucine substitution at residue 509 in the ribonuclease H domain of HIV-1 reverse transcriptase confers zidovudine resistance. Biochemistry 47 (2008) 14020–14027. [DOI] [PMID: 19067547]
5.  Schultz, S.J., Zhang, M., Kelleher, C.D. and Champoux, J.J. Analysis of plus-strand primer selection, removal, and reutilization by retroviral reverse transcriptases. J. Biol. Chem. 275 (2000) 32299–32309. [DOI] [PMID: 10913435]
6.  DeStefano, J.J., Mallaber, L.M., Fay, P.J. and Bambara, R.A. Determinants of the RNase H cleavage specificity of human immunodeficiency virus reverse transcriptase. Nucleic Acids Res. 21 (1993) 4330–4338. [DOI] [PMID: 7692401]
7.  Kati, W.M., Johnson, K.A., Jerva, L.F. and Anderson, K.S. Mechanism and fidelity of HIV reverse transcriptase. J. Biol. Chem. 267 (1992) 25988–25997. [PMID: 1281479]
8.  Palaniappan, C., Fuentes, G.M., Rodriguez-Rodriguez, L., Fay, P.J. and Bambara, R.A. Helix structure and ends of RNA/DNA hybrids direct the cleavage specificity of HIV-1 reverse transcriptase RNase H. J. Biol. Chem. 271 (1996) 2063–2070. [DOI] [PMID: 8567660]
9.  Fu, T.B. and Taylor, J. When retroviral reverse transcriptases reach the end of their RNA templates. J. Virol. 66 (1992) 4271–4278. [PMID: 1376369]
10.  Beilhartz, G.L., Wendeler, M., Baichoo, N., Rausch, J., Le Grice, S. and Gotte, M. HIV-1 reverse transcriptase can simultaneously engage its DNA/RNA substrate at both DNA polymerase and RNase H active sites: implications for RNase H inhibition. J. Mol. Biol. 388 (2009) 462–474. [DOI] [PMID: 19289131]
11.  Huang, H., Chopra, R., Verdine, G.L. and Harrison, S.C. Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance. Science 282 (1998) 1669–1675. [DOI] [PMID: 9831551]
12.  Krug, M.S. and Berger, S.L. Ribonuclease H activities associated with viral reverse transcriptases are endonucleases. Proc. Natl. Acad. Sci. USA 86 (1989) 3539–3543. [DOI] [PMID: 2471188]
13.  Champoux, J.J. and Schultz, S.J. Ribonuclease H: properties, substrate specificity and roles in retroviral reverse transcription. FEBS J. 276 (2009) 1506–1516. [DOI] [PMID: 19228195]
14.  Schultz, S.J. and Champoux, J.J. RNase H activity: structure, specificity, and function in reverse transcription. Virus Res. 134 (2008) 86–103. [DOI] [PMID: 18261820]
15.  Goedken, E.R. and Marqusee, S. Metal binding and activation of the ribonuclease H domain from moloney murine leukemia virus. Protein Eng. 12 (1999) 975–980. [DOI] [PMID: 10585503]
16.  Davies, J.F., 2nd, Hostomska, Z., Hostomsky, Z., Jordan, S.R. and Matthews, D.A. Crystal structure of the ribonuclease H domain of HIV-1 reverse transcriptase. Science 252 (1991) 88–95. [DOI] [PMID: 1707186]
17.  Pari, K., Mueller, G.A., DeRose, E.F., Kirby, T.W. and London, R.E. Solution structure of the RNase H domain of the HIV-1 reverse transcriptase in the presence of magnesium. Biochemistry 42 (2003) 639–650. [DOI] [PMID: 12534276]
[EC 3.1.26.13 created 2009]
 
 
EC 3.2.1.215     
Accepted name: arabinogalactan exo α-(1,3)-α-D-galactosyl-(1→3)-L-arabinofuranosidase (non-reducing end)
Reaction: Hydrolysis of α-D-Galp-(1→3)-L-Araf disaccharides from non-reducing terminals in branches of type II arabinogalactan attached to proteins.
Glossary: Araf = arabinofuranose
Arap = arabinopyranose
Galp = galactopyranose
Other name(s): 3-O-α-D-galactosyl-α-L-arabinofuranosidase
Systematic name: type II arabinogalactan exo α-(1,3)-[α-D-galactosyl-(1→3)-L-arabinofuranose] hydrolase (non-reducing end)
Comments: The enzyme, characterized from the bacterium Bifidobacterium longum, specifically hydrolyses α-D-Galp-(1→3)-L-Araf disaccharides from the non-reducing terminal of arabinogalactan using an exo mode of action. It is particularly active with gum arabic arabinogalactan, a type II arabinogalactan produced by acacia trees. The enzyme can also hydrolyse β-L-Arap-(1→3)-L-Araf disaccharides, but this activity is significantly lower.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Sasaki, Y., Horigome, A., Odamaki, T., Xiao, J.Z., Ishiwata, A., Ito, Y., Kitahara, K. and Fujita, K. Characterization of a novel 3-O-α-D-galactosyl-α-L-arabinofuranosidase for the assimilation of gum arabic AGP in Bifidobacterium longum subsp. longum. Appl. Environ. Microbiol. (2021) . [DOI] [PMID: 33674431]
[EC 3.2.1.215 created 2021]
 
 
EC 3.2.1.223     
Accepted name: arabinogalactan exo α-(1,3)-β-L-arabinopyranosyl-(1→3)-L-arabinofuranosidase (non-reducing end)
Reaction: Hydrolysis of β-L-Arap-(1→3)-L-Araf disaccharides from non-reducing terminals in branches of type II arabinogalactan attached to proteins.
Glossary: Araf = arabinofuranose
Arap = arabinopyranose
Other name(s): 3-O-β-L-arabinopyranosyl-α-L-arabinofuranosidase; AAfase
Systematic name: type II arabinogalactan exo α-(1,3)-[β-L-arabinopyranosyl-(1→3)-L-arabinofuranose] hydrolase (non-reducing end)
Comments: The enzyme, characterized from the bacterium Bifidobacterium pseudocatenulatum, specifically hydrolyses β;-L-Arap-(1→3)-L-Araf disaccharides from the non-reducing terminal of arabinogalactan using an exo mode of action. It is active with arabinogalactan-proteins (AGPs) containing type II arabinogalactans such as gum arabic AGP and larch AGP. The enzyme can also hydrolyse α-D-Galp-(1→3)-L-Araf disaccharides (cf. EC 3.2.1.215) with a much lower activity.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Sasaki, Y., Yanagita, M., Hashiguchi, M., Horigome, A., Xiao, J. Z., Odamaki, T., Kitahara, K. and Fujita, K. Assimilation of arabinogalactan side chains with novel 3-O-β-L-arabinopyranosyl-α-L-arabinofuranosidase in Bifidobacterium pseudocatenulatum. Microbiome Res. Rep. 2:12 (2023). [DOI]
[EC 3.2.1.223 created 2023]
 
 
EC 3.6.3.8      
Transferred entry: Ca2+-transporting ATPase. Now EC 7.2.2.10, Ca2+-transporting ATPase
[EC 3.6.3.8 created 1984 as EC 3.6.1.38, transferred 2000 to EC 3.6.3.8, modified 2001, modified 2011, deleted 2018]
 
 
EC 7.1.3.1     
Accepted name: H+-exporting diphosphatase
Reaction: diphosphate + H2O + H+[side 1] = 2 phosphate + H+[side 2]
Other name(s): H+-PPase; proton-pumping pyrophosphatase; vacuolar H+-pyrophosphatase; hydrogen-translocating pyrophosphatase; proton-pumping dihosphatase
Systematic name: diphosphate phosphohydrolase (H+-transporting)
Comments: This enzyme, found in plants and fungi, couples the energy from diphosphate hydrolysis to active proton translocation across the tonoplast into the vacuole. The enzyme acts cooperatively with cytosolic soluble diphosphatases to regulate the cytosolic diphosphate level.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Rea, P.A. and Poole, R.J. Chromatographic resolution of H+-translocating pyrophosphatase from H+-translocating ATPase of higher plant tonoplast. Plant Physiol. 81 (1986) 126–129. [PMID: 16664761]
2.  Sarafian, V. and Poole, R.J. Purification of an H+-translocating inorganic pyrophosphatase from vacuole membranes of red beet. Plant Physiol. 91 (1989) 34–38. [PMID: 16667022]
3.  Hedrich, R., Kurkdjian, A., Guern, J. and Flugge, U.I. Comparative studies on the electrical properties of the H+ translocating ATPase and pyrophosphatase of the vacuolar-lysosomal compartment. EMBO J. 8 (1989) 2835–2841. [PMID: 2479537]
4.  Segami, S., Tomoyama, T., Sakamoto, S., Gunji, S., Fukuda, M., Kinoshita, S., Mitsuda, N., Ferjani, A. and Maeshima, M. Vacuolar H+-pyrophosphatase and cytosolic soluble pyrophosphatases cooperatively regulate pyrophosphate levels in Arabidopsis thaliana. Plant Cell 30 (2018) 1040–1061. [PMID: 29691313]
[EC 7.1.3.1 created 2018]
 
 
EC 7.2.2.10     
Accepted name: P-type Ca2+ transporter
Reaction: ATP + H2O + Ca2+[side 1] = ADP + phosphate + Ca2+[side 2]
Other name(s): sarcoplasmic reticulum ATPase; sarco(endo)plasmic reticulum Ca2+-ATPase; calcium pump; Ca2+-pumping ATPase; plasma membrane Ca-ATPase; Ca2+-transporting ATPaseP-
Systematic name: ATP phosphohydrolase (P-type, Ca2+-transporting)
Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme family comprises three types of Ca2+-transporting enzymes that are found in the plasma membrane, the sarcoplasmic reticulum, in yeast, and in some bacteria. The enzymes from plasma membrane and from yeast have been shown to transport one ion per ATP hydrolysed whereas those from the sarcoplasmic reticulum transport two ions per ATP hydrolysed. In muscle cells Ca2+ is transported from the cytosol (side 1) into the sarcoplasmic reticulum (side 2).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Schatzmann, H.J. and Vicenzi, F.F. Calcium movements across the membrane of human red cells. J. Physiol. 201 (1969) 369–395. [DOI] [PMID: 4238381]
2.  Inesi, G., Watanabe, T., Coan, C. and Murphy, A. The mechanism of sarcoplasmic reticulum ATPase. Ann. N.Y. Acad. Sci. 402 (1982) 515–532. [DOI] [PMID: 6301340]
3.  Carafoli, E. The Ca2+ pump of the plasma membrane. J. Biol. Chem. 267 (1992) 2115–2118. [PMID: 1310307]
4.  MacLennan, D.H., Rice, W.J. and Green, N.M. The mechanism of Ca2+ transport by sarco(endo)plasmic reticulum Ca2+-ATPases. J. Biol. Chem. 272 (1997) 28815–28818. [DOI] [PMID: 9360942]
5.  Toyoshima, C., Nakasako, M., Nomura, H. and Ogawa, H. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution. Nature 405 (2000) 647–655. [DOI] [PMID: 10864315]
6.  Andersen, J.L., Gourdon, P., Moller, J.V., Morth, J.P. and Nissen, P. Crystallization and preliminary structural analysis of the Listeria monocytogenes Ca(2+)-ATPase LMCA1. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67 (2011) 718–722. [PMID: 21636921]
[EC 7.2.2.10 created 1984 as as EC 3.6.1.38, transferred 2000 to EC 3.6.3.8, modified 2001, modified 2011, transferred 2018 to EC 7.2.2.10]
 
 
EC 7.5.2.12     
Accepted name: ABC-type L-arabinose transporter
Reaction: ATP + H2O + L-arabinose-[arabinose-binding protein][side 1] = ADP + phosphate + L-arabinose[side 2] + [arabinose-binding protein][side 1]
Other name(s): L-arabinose transporting ATPase; L-arabinose ABC transporter; araFGH (gene names)
Systematic name: ATP phosphohydrolase (ABC-type, L-arabinose-importing)
Comments: ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high-affinity uptake of L-arabinose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Scripture, J.B., Voelker, C., Miller, S., O'Donnell, R.T., Polgar, L., Rade, J., Horazdovsky, B.F. and Hogg, R.W. High-affinity L-arabinose transport operon. Nucleotide sequence and analysis of gene products. J. Mol. Biol. 197 (1987) 37–46. [PMID: 2445996]
2.  Horazdovsky, B.F. and Hogg, R.W. Genetic reconstitution of the high-affinity L-arabinose transport system. J. Bacteriol. 171 (1989) 3053–3059. [PMID: 2656640]
[EC 7.5.2.12 created 2019]
 
 


Data © 2001–2024 IUBMB
Web site © 2005–2024 Andrew McDonald