EC |
2.4.1.221 |
Accepted name: |
peptide-O-fucosyltransferase |
Reaction: |
GDP-β-L-fucose + [protein]-(L-serine/L-threonine) = GDP + [protein]-3-O-(α-L-fucosyl)-(L-serine/L-threonine) |
Other name(s): |
GDP-L-fucose:polypeptide fucosyltransferase; GDP-fucose protein O-fucosyltransferase; GDP-fucose:polypeptide fucosyltransferase; POFUT1 (gene name); POFUT2 (gene name) |
Systematic name: |
GDP-β-L-fucose:protein-(L-serine/L-threonine) O-α-L-fucosyltransferase (configuration-inverting) |
Comments: |
The enzyme, found in animals and plants, is involved in the biosynthesis of O-fucosylated proteins. In EGF domains, the attachment of O-linked fucose to serine or threonine occurs within the sequence Cys-Xaa-Xaa-Gly-Gly-Ser/Thr-Cys. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9033-08-3 |
References: |
1. |
Wang, Y. and Spellman, M.W. Purification and characterization of a GDP-fucose:polypeptide fucosyltransferase from Chinese hamster ovary cells. J. Biol. Chem. 273 (1998) 8112–8118. [DOI] [PMID: 9525914] |
2. |
Wang, Y., Shao, L., Shi, S., Harris, R.J., Spellman, M.W., Stanley, P. and Haltiwanger, R.S. Modification of epidermal growth factor-like repeats with O-fucose. Molecular cloning and expression of a novel GDP-fucose protein O-fucosyltransferase. J. Biol. Chem. 276 (2001) 40338–40345. [DOI] [PMID: 11524432] |
3. |
Wang, Y., Lee, G.F., Kelley, R.F. and Spellman, M.W. Identification of a GDP-L-fucose:polypeptide fucosyltransferase and enzymatic addition of O-linked fucose to EGF domains. Glycobiology 6 (1996) 837–842. [DOI] [PMID: 9023546] |
4. |
Hofsteenge, J., Huwiler, K.G., Macek, B., Hess, D., Lawler, J., Mosher, D.F. and Peter-Katalinic, J. C-Mannosylation and O-fucosylation of the thrombospondin type 1 module. J. Biol. Chem. 276 (2001) 6485–6498. [DOI] [PMID: 11067851] |
5. |
Valero-Gonzalez, J., Leonhard-Melief, C., Lira-Navarrete, E., Jimenez-Oses, G., Hernandez-Ruiz, C., Pallares, M.C., Yruela, I., Vasudevan, D., Lostao, A., Corzana, F., Takeuchi, H., Haltiwanger, R.S. and Hurtado-Guerrero, R. A proactive role of water molecules in acceptor recognition by protein O-fucosyltransferase 2. Nat. Chem. Biol. 12 (2016) 240–246. [DOI] [PMID: 26854667] |
6. |
Zentella, R., Sui, N., Barnhill, B., Hsieh, W.P., Hu, J., Shabanowitz, J., Boyce, M., Olszewski, N.E., Zhou, P., Hunt, D.F. and Sun, T.P. The Arabidopsis O-fucosyltransferase SPINDLY activates nuclear growth repressor DELLA. Nat. Chem. Biol. 13 (2017) 479–485. [DOI] [PMID: 28244988] |
7. |
Lopaticki, S., Yang, A.SP., John, A., Scott, N.E., Lingford, J.P., O'Neill, M.T., Erickson, S.M., McKenzie, N.C., Jennison, C., Whitehead, L.W., Douglas, D.N., Kneteman, N.M., Goddard-Borger, E.D. and Boddey, J.A. Protein O-fucosylation in Plasmodium falciparum ensures efficient infection of mosquito and vertebrate hosts. Nat. Commun. 8:561 (2017). [DOI] [PMID: 28916755] |
|
[EC 2.4.1.221 created 2002, modified 2022] |
|
|
|
|
EC |
2.4.1.222 |
Accepted name: |
O-fucosylpeptide 3-β-N-acetylglucosaminyltransferase |
Reaction: |
UDP-N-acetyl-α-D-glucosamine + [protein with EGF-like domain]-3-O-(α-L-fucosyl)-(L-serine/L-threonine) = UDP + [protein with EGF-like domain]-3-O-[N-acetyl-β-D-glucosaminyl-(1→3)-α-L-fucosyl]-(L-serine/L-threonine) |
Glossary: |
EGF = epidermal growth factor
EGF-like domain = an evolutionary conserved domain containing 30 to 40 amino-acid residues first described from epidermal growth factor |
Other name(s): |
O-fucosylpeptide β-1,3-N-acetylglucosaminyltransferase; fringe; UDP-D-GlcNAc:O-L-fucosylpeptide 3-β-N-acetyl-D-glucosaminyltransferase |
Systematic name: |
UDP-N-acetyl-α-D-glucosamine:[protein with EGF-like domain]-3-O-(α-L-fucosyl)-(L-serine/L-threonine) 3-β-N-acetyl-D-glucosaminyltransferase (configuration-inverting) |
Comments: |
The enzyme, found in animals and plants, is involved in the biosynthesis of the tetrasaccharides α-Neu5Ac-(2→3)-β-D-Gal-(1→4)-β-D-GlcNAc-(1→3)-α-L-Fuc and α-Neu5Ac-(2→6)-β-D-Gal-(1→4)-β-D-GlcNAc-(1→3)-α-L-Fuc, which are attached to L-Ser or L-Thr residues within the sequence Cys-Xaa-Xaa-Gly-Gly-Ser/Thr-Cys in EGF-like domains in Notch and Factor-X proteins, respectively. The substrate is provided by EC 2.4.1.221, peptide-O-fucosyltransferase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 299203-70-6 |
References: |
1. |
Moloney, D.J., Panin, V.M., Johnston, S.H., Chen, J., Shao, L., Wilson, R., Wang, Y., Stanley, P., Irvine, K.D., Haltiwanger, R.S. and Vogt, T.F. Fringe is a glycosyltransferase that modifies Notch. Nature 406 (2000) 369–375. [DOI] [PMID: 10935626] |
2. |
Bruckner, K., Perez, L., Clausen, H. and Cohen, S. Glycosyltransferase activity of Fringe modulates Notch-Delta interactions. Nature 406 (2000) 411–415. [DOI] [PMID: 10935637] |
3. |
Rampal, R., Li, A.S., Moloney, D.J., Georgiou, S.A., Luther, K.B., Nita-Lazar, A. and Haltiwanger, R.S. Lunatic fringe, manic fringe, and radical fringe recognize similar specificity determinants in O-fucosylated epidermal growth factor-like repeats. J. Biol. Chem. 280 (2005) 42454–42463. [DOI] [PMID: 16221665] |
|
[EC 2.4.1.222 created 2002, modified 2022] |
|
|
|
|
EC |
2.4.1.376 |
Accepted name: |
EGF-domain serine glucosyltransferase |
Reaction: |
UDP-α-D-glucose + [protein with EGF-like domain]-L-serine = UDP + [protein with EGF-like domain]-3-O-(β-D-glucosyl)-L-serine |
Other name(s): |
POGLUT1 (gene name) (ambiguous); rumi (gene name) (ambiguous) |
Systematic name: |
UDP-α-D-glucose:[protein with EGF-like domain]-L-serine O-β-glucosyltransferase (configuration-inverting) |
Comments: |
The enzyme, found in animals and insects, is involved in the biosynthesis of the α-D-xylosyl-(1→3)-α-D-xylosyl-(1→3)-β-D-glucosyl trisaccharide on epidermal growth factor-like (EGF-like) domains. Glycosylation takes place at the serine in the C-X-S-X-P-C motif. The enzyme is bifunctional also being active with UDP-α-xylose as donor (EC 2.4.2.63, EGF-domain serine xylosyltransferase). When present on Notch proteins, the trisaccharide functions as a modulator of the signalling activity of this protein. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Li, Z., Fischer, M., Satkunarajah, M., Zhou, D., Withers, S.G. and Rini, J.M. Structural basis of Notch O-glucosylation and O-xylosylation by mammalian protein-O-glucosyltransferase 1 (POGLUT1). Nat. Commun. 8:185 (2017). [PMID: 28775322] |
|
[EC 2.4.1.376 created 2020] |
|
|
|
|
EC |
2.4.2.42 |
Accepted name: |
UDP-D-xylose:β-D-glucoside α-1,3-D-xylosyltransferase |
Reaction: |
UDP-α-D-xylose + [protein with EGF-like domain]-3-O-(β-D-glucosyl)-L-serine = UDP + [protein with EGF-like domain]-3-O-[α-D-xylosyl-(1→3)-β-D-glucosyl]-L-serine |
Other name(s): |
β-glucoside α-1,3-xylosyltransferase; UDP-α-D-xylose:β-D-glucoside 3-α-D-xylosyltransferase; GXYLT1 (gene name); GXYLT2 (gene name) |
Systematic name: |
UDP-α-D-xylose:[protein with EGF-like domain]-3-O-(β-D-glucosyl)-L-serine 3-α-D-xylosyltransferase (configuration-retaining) |
Comments: |
The enzyme, found in animals and insects, is involved in the biosynthesis of the α-D-xylosyl-(1→3)-α-D-xylosyl-(1→3)-β-D-glucosyl trisaccharide on epidermal growth factor-like (EGF-like) domains [2,3]. When present on Notch proteins, the trisaccharide functions as a modulator of the signalling activity of this protein. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Omichi, K., Aoki, K., Minamida, S. and Hase, S. Presence of UDP-D-xylose: β-D-glucoside α-1,3-D-xylosyltransferase involved in the biosynthesis of the Xyl α 1-3Glc β-Ser structure of glycoproteins in the human hepatoma cell line HepG2. Eur. J. Biochem. 245 (1997) 143–146. [DOI] [PMID: 9128735] |
2. |
Ishimizu, T., Sano, K., Uchida, T., Teshima, H., Omichi, K., Hojo, H., Nakahara, Y. and Hase, S. Purification and substrate specificity of UDP-D-xylose:β-D-glucoside α-1,3-D-xylosyltransferase involved in the biosynthesis of the Xyl α1-3Xyl α1-3Glc β1-O-Ser on epidermal growth factor-like domains. J. Biochem. 141 (2007) 593–600. [DOI] [PMID: 17317689] |
3. |
Sethi, M.K., Buettner, F.F., Krylov, V.B., Takeuchi, H., Nifantiev, N.E., Haltiwanger, R.S., Gerardy-Schahn, R. and Bakker, H. Identification of glycosyltransferase 8 family members as xylosyltransferases acting on O-glucosylated notch epidermal growth factor repeats. J. Biol. Chem. 285 (2010) 1582–1586. [PMID: 19940119] |
|
[EC 2.4.2.42 created 2010, modified 2020] |
|
|
|
|
EC |
2.4.2.62 |
Accepted name: |
xylosyl α-1,3-xylosyltransferase |
Reaction: |
UDP-α-D-xylose + [protein with EGF-like domain]-3-O-[α-D-xylosyl-(1→3)-β-D-glucosyl]-L-serine = UDP + [protein with EGF-like domain]-3-O-[α-D-xylosyl-(1→3)-α-D-xylosyl-(1→3)-β-D-glucosyl]-L-serine |
Other name(s): |
XXYLT1 (gene name) |
Systematic name: |
UDP-α-D-xylose:[EGF-like domain protein]-3-O-[α-D-xylosyl-(1→3)-β-D-glucosyl]-L-serine 3-α-D-xylosyltransferase (configuration-retaining) |
Comments: |
The enzyme, found in animals and insects, is involved in the biosynthesis of the α-D-xylosyl-(1→3)-α-D-xylosyl-(1→3)-β-D-glucosyl trisaccharide on epidermal growth factor-like (EGF-like) domains. When present on Notch proteins, the trisaccharide functions as a modulator of the signalling activity of this protein. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Minamida, S., Aoki, K., Natsuka, S., Omichi, K., Fukase, K., Kusumoto, S. and Hase, S. Detection of UDP-D-xylose: α-D-xyloside α 1-→3xylosyltransferase activity in human hepatoma cell line HepG2. J. Biochem. 120 (1996) 1002–1006. [PMID: 8982869] |
2. |
Sethi, M.K., Buettner, F.F., Ashikov, A., Krylov, V.B., Takeuchi, H., Nifantiev, N.E., Haltiwanger, R.S., Gerardy-Schahn, R. and Bakker, H. Molecular cloning of a xylosyltransferase that transfers the second xylose to O-glucosylated epidermal growth factor repeats of notch. J. Biol. Chem. 287 (2012) 2739–2748. [PMID: 22117070] |
3. |
Yu, H., Takeuchi, M., LeBarron, J., Kantharia, J., London, E., Bakker, H., Haltiwanger, R.S., Li, H. and Takeuchi, H. Notch-modifying xylosyltransferase structures support an SNi-like retaining mechanism. Nat. Chem. Biol. 11 (2015) 847–854. [PMID: 26414444] |
|
[EC 2.4.2.62 created 2020] |
|
|
|
|
EC |
2.4.2.63 |
Accepted name: |
EGF-domain serine xylosyltransferase |
Reaction: |
UDP-α-D-xylose + [protein with EGF-like domain]-L-serine = UDP + [protein with EGF-like domain]-3-O-(β-D-xylosyl)-L-serine |
Other name(s): |
POGLUT1 (gene name) (ambiguous); rumi (gene name) (ambiguous) |
Systematic name: |
UDP-α-D-xylose:[protein with EGF-like domain]-L-serine O-β-xylosyltransferase (configuration-inverting) |
Comments: |
The enzyme, found in animals and insects, xylosylates at the serine in the C-X-S-X-P-C motif of epidermal growth factor-like (EGF-like) domains. The enzyme is bifunctional also being active with UDP-α-glucose as donor (EC 2.4.1.376, EGF-domain serine glucosyltransferase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Li, Z., Fischer, M., Satkunarajah, M., Zhou, D., Withers, S.G. and Rini, J.M. Structural basis of Notch O-glucosylation and O-xylosylation by mammalian protein-O-glucosyltransferase 1 (POGLUT1). Nat. Commun. 8:185 (2017). [PMID: 28775322] |
|
[EC 2.4.2.63 created 2020] |
|
|
|
|
EC |
2.7.7.82 |
Accepted name: |
CMP-N,N′-diacetyllegionaminic acid synthase |
Reaction: |
CTP + N,N′-diacetyllegionaminate = CMP-N,N′-diacetyllegionaminate + diphosphate |
|
For diagram of legionaminic acid biosynthesis, click here |
Glossary: |
legionaminate = 5,7-diamino-3,5,7,9-tetradeoxy-D-glycero-D-galacto-non-2-ulosonate |
Other name(s): |
CMP-N,N′-diacetyllegionaminic acid synthetase; neuA (gene name); legF (gene name) |
Systematic name: |
CTP:N,N′-diacetyllegionaminate cytidylyltransferase |
Comments: |
Isolated from the bacteria Legionella pneumophila and Campylobacter jejuni. Involved in biosynthesis of legionaminic acid, a sialic acid-like derivative that is incorporated into virulence-associated cell surface glycoconjugates which may include lipopolysaccharide (LPS), capsular polysaccharide, pili and flagella. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Glaze, P.A., Watson, D.C., Young, N.M. and Tanner, M.E. Biosynthesis of CMP-N,N′-diacetyllegionaminic acid from UDP-N,N′-diacetylbacillosamine in Legionella pneumophila. Biochemistry 47 (2008) 3272–3282. [DOI] [PMID: 18275154] |
2. |
Schoenhofen, I.C., Vinogradov, E., Whitfield, D.M., Brisson, J.R. and Logan, S.M. The CMP-legionaminic acid pathway in Campylobacter: biosynthesis involving novel GDP-linked precursors. Glycobiology 19 (2009) 715–725. [DOI] [PMID: 19282391] |
|
[EC 2.7.7.82 created 2012] |
|
|
|
|
EC |
2.7.10.1 |
Accepted name: |
receptor protein-tyrosine kinase |
Reaction: |
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate |
Other name(s): |
AATK; AATYK; AATYK2; AATYK3; ACH; ALK; anaplastic lymphoma kinase; ARK; ATP:protein-tyrosine O-phosphotransferase (ambiguous); AXL; Bek; Bfgfr; BRT; Bsk; C-FMS; CAK; CCK4; CD115; CD135; CDw135; Cek1; Cek10; Cek11; Cek2; Cek3; Cek5; Cek6; Cek7; CFD1; CKIT; CSF1R; DAlk; DDR1; DDR2; Dek; DKFZp434C1418; Drosophila Eph kinase; DRT; DTK; Ebk; ECK; EDDR1; Eek; EGFR; Ehk2; Ehk3; Elk; EPH; EPHA1; EPHA2; EPHA6; EPHA7; EPHA8; EPHB1; EPHB2; EPHB3; EPHB4; EphB5; ephrin-B3 receptor tyrosine kinase; EPHT; EPHT2; EPHT3; EPHX; ERBB; ERBB1; ERBB2; ERBB3; ERBB4; ERK; Eyk; FGFR1; FGFR2; FGFR3; FGFR4; FLG; FLK1; FLK2; FLT1; FLT2; FLT3; FLT4; FMS; Fv2; HBGFR; HEK11; HEK2; HEK3; HEK5; HEK6; HEP; HER2; HER3; HER4; HGFR; HSCR1; HTK; IGF1R; INSR; INSRR; insulin receptor protein-tyrosine kinase; IR; IRR; JTK12; JTK13; JTK14; JWS; K-SAM; KDR; KGFR; KIA0641; KIAA1079; KIAA1459; Kil; Kin15; Kin16; KIT; KLG; LTK; MCF3; Mdk1; Mdk2; Mdk5; MEhk1; MEN2A/B; Mep; MER; MERTK; MET; Mlk1; Mlk2; Mrk; MST1R; MTC1; MUSK; Myk1; N-SAM; NEP; NET; Neu; neurite outgrowth regulating kinase; NGL; NOK; nork; novel oncogene with kinase-domain; Nsk2; NTRK1; NTRK2; NTRK3; NTRK4; NTRKR1; NTRKR2; NTRKR3; Nuk; NYK; PCL; PDGFR; PDGFRA; PDGFRB; PHB6; protein-tyrosine kinase (ambiguous); protein tyrosine kinase (ambiguous); PTK; PTK3; PTK7; receptor protein tyrosine kinase; RET; RON; ROR1; ROR2; ROS1; RSE; RTK; RYK; SEA; Sek2; Sek3; Sek4; Sfr; SKY; STK (ambiguous); STK1; TEK; TIE; TIE1; TIE2; TIF; TKT; TRK; TRKA; TRKB; TRKC; TRKE; TYK1; TYRO10; Tyro11; TYRO3; Tyro5; Tyro6; TYRO7; UFO; VEGFR1; VEGFR2; VEGFR3; Vik; YK1; Yrk |
Systematic name: |
ATP:[protein]-L-tyrosine O-phosphotransferase (receptor-type) |
Comments: |
The receptor protein-tyrosine kinases, which can be defined as having a transmembrane domain, are a large and diverse multigene family found only in Metazoans [1]. In the human genome, 58 receptor-type protein-tyrosine kinases have been identified and these are distributed into 20 subfamilies. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Robinson, D.R., Wu, Y.M. and Lin, S.F. The protein tyrosine kinase family of the human genome. Oncogene 19 (2000) 5548–5557. [DOI] [PMID: 11114734] |
2. |
Iwahara, T., Fujimoto, J., Wen, D., Cupples, R., Bucay, N., Arakawa, T., Mori, S., Ratzkin, B. and Yamamoto, T. Molecular characterization of ALK, a receptor tyrosine kinase expressed specifically in the nervous system. Oncogene 14 (1997) 439–449. [DOI] [PMID: 9053841] |
3. |
Lorén, C.E., Scully, A., Grabbe, C., Edeen, P.T., Thomas, J., McKeown, M., Hunter, T. and Palmer, R.H. Identification and characterization of DAlk: a novel Drosophila melanogaster RTK which drives ERK activation in vivo. Genes. Cell 6 (2001) 531–544. [DOI] [PMID: 11442633] |
|
[EC 2.7.10.1 created 1984 as EC 2.7.1.112, part transferred 2005 to EC 2.7.10.1] |
|
|
|
|
EC |
3.4.21.105 |
Accepted name: |
rhomboid protease |
Reaction: |
Cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains |
Comments: |
These endopeptidases are multi-spanning membrane proteins. Their catalytic site is embedded within the membrane and they cleave type-1 transmembrane domains. A catalytic dyad is involved in proteolysis rather than a catalytic triad, as was thought previously [14]. They are important for embryo development in Drosophila melanogaster. Rhomboid is a key regulator of EGF receptor signalling and is responsible for cleaving Spitz, the main ligand of the Drosophila EGF receptor pathway. Belongs in peptidase family S54. Parasite-encoded rhomboid enzymes are also important for invasion of host cells by Toxoplasma and the malaria parasite. Rhomboids are widely conserved from bacteria to archaea to humans [9,13]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 713145-02-9 |
References: |
1. |
Urban, S. and Wolfe, M.S. Reconstitution of intramembrane proteolysis in vitro reveals that pure rhomboid is sufficient for catalysis and specificity. Proc. Natl. Acad. Sci. USA 102 (2005) 1883–1888. [DOI] [PMID: 15684070] |
2. |
Brossier, F., Jewett, T.J., Sibley, L.D. and Urban, S. A spatially localized rhomboid protease cleaves cell surface adhesins essential for invasion by Toxoplasma. Proc. Natl. Acad. Sci. USA 102 (2005) 4146–4151. [DOI] [PMID: 15753289] |
3. |
Herlan, M., Bornhovd, C., Hell, K., Neupert, W. and Reichert, A.S. Alternative topogenesis of Mgm1 and mitochondrial morphology depend on ATP and a functional import motor. J. Cell Biol. 165 (2004) 167–173. [DOI] [PMID: 15096522] |
4. |
Pascall, J.C. and Brown, K.D. Intramembrane cleavage of ephrinB3 by the human rhomboid family protease, RHBDL 2. Biochem. Biophys. Res. Commun. 317 (2004) 244–252. [DOI] [PMID: 15047175] |
5. |
Sik, A., Passer, B.J., Koonin, E.V. and Pellegrini, L. Self-regulated cleavage of the mitochondrial intramembrane-cleaving protease PARL yields Pβ, a nuclear-targeted peptide. J. Biol. Chem. 279 (2004) 15323–15329. [DOI] [PMID: 14732705] |
6. |
Urban, S. and Freeman, M. Substrate specificity of Rhomboid intramembrane proteases is governed by helix-breaking residues in the substrate transmembrane domain. Mol. Cell 11 (2003) 1425–1434. [DOI] [PMID: 12820957] |
7. |
Herlan, M., Vogel, F., Bornhovd, C., Neupert, W. and Reichert, A.S. Processing of Mgm1 by the rhomboid-type protease Pcp1 is required for maintenance of mitochondrial morphology and of mitochondrial DNA. J. Biol. Chem. 278 (2003) 27781–27788. [DOI] [PMID: 12707284] |
8. |
McQuibban, G.A., Saurya, S. and Freeman, M. Mitochondrial membrane remodelling regulated by a conserved rhomboid protease. Nature 423 (2003) 537–541. [DOI] [PMID: 12774122] |
9. |
Koonin, E.V., Makarova, K.S., Rogozin, I.B., Davidovic, L., Letellier, M.C. and Pellegrini, L. The rhomboids: a nearly ubiquitous family of intramembrane serine proteases that probably evolved by multiple ancient horizontal gene transfers. Genome Biol. 4 (2003) R19. [DOI] [PMID: 12620104] |
10. |
Urban, S. and Freeman, M. Intramembrane proteolysis controls diverse signalling pathways throughout evolution. Curr. Opin. Genet. Dev. 12 (2002) 512–518. [DOI] [PMID: 12200155] |
11. |
Urban, S., Schlieper, D. and Freeman, M. Conservation of intramembrane proteolytic activity and substrate specificity in prokaryotic and eukaryotic Rhomboids. Curr. Biol. 12 (2002) 1507–1512. [DOI] [PMID: 12225666] |
12. |
Urban, S., Lee, J.R. and Freeman, M. A family of Rhomboid intramembrane proteases activates all Drosophila membrane-tethered EGF-like ligands. EMBO J. 21 (2002) 4277–4286. [DOI] [PMID: 12169630] |
13. |
Urban, S., Lee, J.R. and Freeman, M. Drosophila Rhomboid-1 defines a family of putative intramembrane serine proteases. Cell 107 (2001) 173–182. [DOI] [PMID: 11672525] |
14. |
Lemberg, M.K., Menendez, J., Misik, A., Garcia, M., Koth, C.M. and Freeman, M. Mechanism of intramembrane proteolysis investigated with purified rhomboid proteases. EMBO J. 24 (2005) 464–472. [DOI] [PMID: 15616571] |
15. |
Wang, Y., Zhang, Y. and Ha, Y. Crystal structure of a rhomboid family intramembrane protease. Nature 444 (2006) 179–180. [DOI] [PMID: 17051161] |
|
[EC 3.4.21.105 created 2005] |
|
|
|
|