The Enzyme Database

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EC 1.1.1.238     
Accepted name: 12β-hydroxysteroid dehydrogenase
Reaction: 3α,7α,12β-trihydroxy-5β-cholan-24-oate + NADP+ = 3α,7α-dihydroxy-12-oxo-5β-cholan-24-oate + NADPH + H+
Other name(s): 12β-hydroxy steroid (nicotinamide adenine dinucleotide phosphate) dehydrogenase
Systematic name: 12β-hydroxysteroid:NADP+ 12-oxidoreductase
Comments: Acts on a number of bile acids, both in their free and conjugated forms.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 118390-62-8
References:
1.  Edenharder, R. and Pfützner, A. Characterization of NADP-dependent 12β-hydroxysteroid dehydrogenase from Clostridium paraputrificum. Biochim. Biophys. Acta 962 (1988) 362–370. [DOI] [PMID: 3167086]
[EC 1.1.1.238 created 1992]
 
 
EC 1.1.1.358     
Accepted name: 2-dehydropantolactone reductase
Reaction: (R)-pantolactone + NADP+ = 2-dehydropantolactone + NADPH + H+
Other name(s): 2-oxopantoyl lactone reductase; 2-ketopantoyl lactone reductase; ketopantoyl lactone reductase; 2-dehydropantoyl-lactone reductase
Systematic name: (R)-pantolactone:NADP+ oxidoreductase
Comments: The enzyme participates in an alternative pathway for biosynthesis of (R)-pantothenate (vitamin B5). This entry covers enzymes whose stereo specificity for NADP+ is not known. cf. EC 1.1.1.168 2-dehydropantolactone reductase (Re-specific) and EC 1.1.1.214, 2-dehydropantolactone reductase (Si-specific).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Hata, H., Shimizu, S., Hattori, S. and Yamada, H. Ketopantoyl-lactone reductase from Candida parapsilosis: purification and characterization as a conjugated polyketone reductase. Biochim. Biophys. Acta 990 (1989) 175–181. [DOI] [PMID: 2644973]
[EC 1.1.1.358 created 2013]
 
 
EC 1.1.1.430     
Accepted name: D-xylose reductase (NADH)
Reaction: xylitol + NAD+ = D-xylose + NADH + H+
Other name(s): XYL1 (gene name) (ambiguous)
Systematic name: xylitol:NAD+ oxidoreductase
Comments: Xylose reductases catalyse the reduction of xylose to xylitol, the initial reaction in the fungal D-xylose degradation pathway. Most of the enzymes exhibit a strict requirement for NADPH (cf. EC 1.1.1.431, D-xylose reductase (NADPH)). Some D-xylose reductases have dual cosubstrate specificity, though they still prefer NADPH to NADH (cf. EC 1.1.1.307, D-xylose reductase [NAD(P)H]). The enzyme from Candida parapsilosis is a rare example of a xylose reductase that significantly prefers NADH, with Km and Vmax values for NADH being 10-fold lower and 10-fold higher, respectively, than for NADPH.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Lee, J.K., Koo, B.S. and Kim, S.Y. Cloning and characterization of the xyl1 gene, encoding an NADH-preferring xylose reductase from Candida parapsilosis, and its functional expression in Candida tropicalis. Appl. Environ. Microbiol. 69 (2003) 6179–6188. [DOI] [PMID: 14532079]
[EC 1.1.1.430 created 2022]
 
 
EC 1.13.12.6     
Accepted name: Cypridina-luciferin 2-monooxygenase
Reaction: Cypridina luciferin + O2 = oxidized Cypridina luciferin + CO2 + hν
For diagram of reaction, click here
Glossary: Cypridina-luciferin = (3-{3,7-dihydro-6-(1H-indol-3-yl)-2-[(S)-1-methylpropyl]-3-oxoimidazo[1,2-a]pyrazin-8-yl}propyl)guanidine
Other name(s): Cypridina-type luciferase; luciferase (Cypridina luciferin); Cypridina luciferase
Systematic name: Cypridina-luciferin:oxygen 2-oxidoreductase (decarboxylating)
Comments: Cypridina is a bioluminescent crustacea. The luciferins (and presumably the luciferases, since they cross-react) of some luminous fish (e.g. Apogon, Parapriacanthus, Porichthys) are apparently similar. The enzyme may be assayed by measurement of light emission.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 61969-99-1
References:
1.  Cormier, M.J., Crane, J.M., Jr. and Nakano, Y. 1Evidence for the identity of the luminescent systems of Porichthys porosissimus (fish) and Cypridina hilgendorfii (crustacean). Biochem. Biophys. Res. Commun. 29 (1967) 747–752. [DOI] [PMID: 5624784]
2.  Karpetsky, T.P. and White, E.H. The synthesis of Cypridina etioluciferamine and the proof of the structure of Cypridina luciferin. Tetrahedron 29 (1973) 3761–3773.
3.  Kishi, Y., Goto, T., Hirata, Y., Shiromura, O. and Johnson, F.H. Cypridina bioluminescence. I. Structure of Cypridina luciferin. Tetrahedron Lett. (1966) 3427–3436.
4.  Tsuji, F.I., Lynch, R.V. and Stevens, C.L. Some properties of luciferase from the bioluminescent crustacean, Cypridina hilgendorfii. Biochemistry 13 (1974) 5204–5209. [PMID: 4433517]
[EC 1.13.12.6 created 1976, modified 1982]
 
 
EC 1.14.13.64     
Accepted name: 4-hydroxybenzoate 1-hydroxylase
Reaction: 4-hydroxybenzoate + NAD(P)H + 2 H+ + O2 = hydroquinone + NAD(P)+ + H2O + CO2
Other name(s): 4-hydroxybenzoate 1-monooxygenase
Systematic name: 4-hydroxybenzoate,NAD(P)H:oxygen oxidoreductase (1-hydroxylating, decarboxylating)
Comments: Requires FAD. The enzyme from Candida parapsilosis is specific for 4-hydroxybenzoate derivatives and prefers NADH to NADPH as electron donor.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, CAS registry number: 134214-78-1
References:
1.  van Berkel, W.J.H., Eppink, M.H.M., Middelhoven, W.J., Vervoort, J. and Rietjens, I.M.C.M. Catabolism of 4-hydroxybenzoate in Candida parapsilosis proceeds through initial oxidative decarboxylation by a FAD-dependent 4-hydroxybenzoate 1-hydroxylase. FEMS Microbiol. Lett. 121 (1994) 207–216. [DOI] [PMID: 7926672]
[EC 1.14.13.64 created 1999]
 
 
EC 2.1.1.137     
Accepted name: arsenite methyltransferase
Reaction: (1) S-adenosyl-L-methionine + arsenic triglutathione + thioredoxin + 2 H2O = S-adenosyl-L-homocysteine + methylarsonous acid + 3 glutathione + thioredoxin disulfide
(2) 2 S-adenosyl-L-methionine + arsenic triglutathione + 2 thioredoxin + H2O = S-adenosyl-L-homocysteine + dimethylarsinous acid + 3 glutathione + 2 thioredoxin disulfide
(3) 3 S-adenosyl-L-methionine + arsenic triglutathione + 3 thioredoxin = S-adenosyl-L-homocysteine + trimethylarsane + 3 glutathione + 3 thioredoxin disulfide
For diagram of arsenate catabolism, click here
Other name(s): AS3MT (gene name); arsM (gene name); S-adenosyl-L-methionine:arsenic(III) methyltransferase; S-adenosyl-L-methionine:methylarsonite As-methyltransferase; methylarsonite methyltransferase
Systematic name: S-adenosyl-L-methionine:arsenous acid As-methyltransferase
Comments: An enzyme responsible for synthesis of trivalent methylarsenical antibiotics in microbes [11] or detoxification of inorganic arsenous acid in animals. The in vivo substrate is arsenic triglutathione or similar thiol (depending on the organism) [6], from which the arsenic is transferred to the enzyme forming bonds with the thiol groups of three cysteine residues [10] via a disulfide bond cascade pathway [7, 8]. Most of the substrates undergo two methylations and are converted to dimethylarsinous acid [9]. However, a small fraction are released earlier as methylarsonous acid, and a smaller amount proceeds via a third methylation, resulting in the volatile product trimethylarsane. Methylation involves temporary oxidation to arsenic(V) valency, followed by reduction back to arsenic(III) valency using electrons provided by thioredoxin or a similar reduction system. The arsenic(III) products are quickly oxidized in the presence of oxygen to the corresponding arsenic(V) species.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 167140-41-2
References:
1.  Zakharyan, R.A., Wu, Y., Bogdan, G.M. and Aposhian, H.V. Enzymatic methylation of arsenic compounds: assay, partial purification, and properties of arsenite methyltransferase and monomethylarsonic acid methyltransferase of rabbit liver. Chem. Res. Toxicol. 8 (1995) 1029–1038. [PMID: 8605285]
2.  Zakharyan, R.A., Wildfang, E. and Aposhian, H.V. Enzymatic methylation of arsenic compounds. III. The marmoset and tamarin, but not the rhesus, monkeys are deficient in methyltransferases that methylate inorganic arsenic. Toxicol. Appl. Pharmacol. 140 (1996) 77–84. [DOI] [PMID: 8806872]
3.  Zakharyan, R.A. and Aposhian, H.V. Enzymatic reduction of arsenic compounds in mammalian systems: the rate-limiting enzyme of rabbit liver arsenic biotransformation is MMA(V) reductase. Chem. Res. Toxicol. 12 (1999) 1278–1283. [DOI] [PMID: 10604879]
4.  Zakharyan, R.A., Ayala-Fierro, F., Cullen, W.R., Carter, D.M. and Aposhian, H.V. Enzymatic methylation of arsenic compounds. VII. Monomethylarsonous acid (MMAIII) is the substrate for MMA methyltransferase of rabbit liver and human hepatocytes. Toxicol. Appl. Pharmacol. 158 (1999) 9–15. [DOI] [PMID: 10387927]
5.  Lin, S., Shi, Q., Nix, F.B., Styblo, M., Beck, M.A., Herbin-Davis, K.M., Hall, L.L., Simeonsson, J.B. and Thomas, D.J. A novel S-adenosyl-L-methionine:arsenic(III) methyltransferase from rat liver cytosol. J. Biol. Chem. 277 (2002) 10795–10803. [DOI] [PMID: 11790780]
6.  Hayakawa, T., Kobayashi, Y., Cui, X. and Hirano, S. A new metabolic pathway of arsenite: arsenic-glutathione complexes are substrates for human arsenic methyltransferase Cyt19. Arch Toxicol 79 (2005) 183–191. [DOI] [PMID: 15526190]
7.  Dheeman, D.S., Packianathan, C., Pillai, J.K. and Rosen, B.P. Pathway of human AS3MT arsenic methylation. Chem. Res. Toxicol. 27 (2014) 1979–1989. [DOI] [PMID: 25325836]
8.  Marapakala, K., Packianathan, C., Ajees, A.A., Dheeman, D.S., Sankaran, B., Kandavelu, P. and Rosen, B.P. A disulfide-bond cascade mechanism for arsenic(III) S-adenosylmethionine methyltransferase. Acta Crystallogr. D Biol. Crystallogr. 71 (2015) 505–515. [DOI] [PMID: 25760600]
9.  Yang, H.C. and Rosen, B.P. New mechanisms of bacterial arsenic resistance. Biomed J 39 (2016) 5–13. [DOI] [PMID: 27105594]
10.  Packianathan, C., Kandavelu, P. and Rosen, B.P. The structure of an As(III) S-adenosylmethionine methyltransferase with 3-coordinately bound As(III) depicts the first step in catalysis. Biochemistry 57 (2018) 4083–4092. [DOI] [PMID: 29894638]
11.  Chen, J., Yoshinaga, M. and Rosen, B.P. The antibiotic action of methylarsenite is an emergent property of microbial communities. Mol. Microbiol. 111 (2019) 487–494. [DOI] [PMID: 30520200]
[EC 2.1.1.137 created 2000, (EC 2.1.1.138 incorporated 2003), modified 2003, modified 2021]
 
 
EC 2.5.1.114     
Accepted name: tRNAPhe (4-demethylwyosine37-C7) aminocarboxypropyltransferase
Reaction: S-adenosyl-L-methionine + 4-demethylwyosine37 in tRNAPhe = S-methyl-5′-thioadenosine + 7-[(3S)-3-amino-3-carboxypropyl]-4-demethylwyosine37 in tRNAPhe
For diagram of wyosine biosynthesis, click here
Glossary: 4-demethylwyosine = imG-14 = 6-methyl-3-(β-D-ribofuranosyl)-3,5-dihydro-9H-imidazo[1,2-a]purin-9-one
7-[(3S)-3-amino-3-carboxypropyl]-4-demethylwyosine = yW-89
Other name(s): TYW2; tRNA-yW synthesizing enzyme-2; TRM12 (gene name); taw2 (gene name)
Systematic name: S-adenosyl-L-methionine:tRNAPhe (4-demethylwyosine37-C7)-[(3S)-3-amino-3-carboxypropyl]transferase
Comments: The enzyme, which is found in all eukaryotes and in the majority of Euryarchaeota (but not in the Crenarchaeota), is involved in the hypermodification of the guanine nucleoside at position 37 of tRNA leading to formation of assorted wye bases. This modification is essential for translational reading-frame maintenance. The eukaryotic enzyme is involved in biosynthesis of the tricyclic base wybutosine, which is found only in tRNAPhe.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Umitsu, M., Nishimasu, H., Noma, A., Suzuki, T., Ishitani, R. and Nureki, O. Structural basis of AdoMet-dependent aminocarboxypropyl transfer reaction catalyzed by tRNA-wybutosine synthesizing enzyme, TYW2. Proc. Natl. Acad. Sci. USA 106 (2009) 15616–15621. [DOI] [PMID: 19717466]
2.  Rodriguez, V., Vasudevan, S., Noma, A., Carlson, B.A., Green, J.E., Suzuki, T. and Chandrasekharappa, S.C. Structure-function analysis of human TYW2 enzyme required for the biosynthesis of a highly modified Wybutosine (yW) base in phenylalanine-tRNA. PLoS One 7:e39297 (2012). [DOI] [PMID: 22761755]
3.  de Crecy-Lagard, V., Brochier-Armanet, C., Urbonavicius, J., Fernandez, B., Phillips, G., Lyons, B., Noma, A., Alvarez, S., Droogmans, L., Armengaud, J. and Grosjean, H. Biosynthesis of wyosine derivatives in tRNA: an ancient and highly diverse pathway in Archaea. Mol. Biol. Evol. 27 (2010) 2062–2077. [DOI] [PMID: 20382657]
[EC 2.5.1.114 created 2013]
 
 
EC 2.7.1.232     
Accepted name: levoglucosan kinase
Reaction: ATP + levoglucosan + H2O = ADP + D-glucose 6-phosphate
Glossary: levoglucosan = 1,6-anhydro-β-D-glucopyranose
Systematic name: ATP:1,6-anhydro-β-D-glucopyranose 6-phosphotransferase (hydrolyzing)
Comments: Levoglucosan is formed from the pyrolysis of carbohydrates such as starch and cellulose and is an important molecular marker for pollution from biomass burning. The enzyme, found in yeast and fungi, requires a magnesium ion. cf. EC 1.1.1.425, levoglucosan dehydrogenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Zhuang, X. and Zhang, H. Identification, characterization of levoglucosan kinase, and cloning and expression of levoglucosan kinase cDNA from Aspergillus niger CBX-209 in Escherichia coli. Protein Expr. Purif. 26 (2002) 71–81. [PMID: 12356473]
2.  Dai, J., Yu, Z., He, Y., Zhang, L., Bai, Z., Dong, Z., Du, Y. and Zhang, H. Cloning of a novel levoglucosan kinase gene from Lipomyces starkeyi and its expression in Escherichia coli. World J. Microbiol. Biotechnol. 25 (2009) 1589–1595. [DOI]
3.  Layton, D.S., Ajjarapu, A., Choi, D.W. and Jarboe, L.R. Engineering ethanologenic Escherichia coli for levoglucosan utilization. Bioresour. Technol. 102 (2011) 8318–8322. [DOI] [PMID: 21719279]
4.  Islam, Z.U., Zhisheng, Y., Hassan el, B., Dongdong, C. and Hongxun, Z. Microbial conversion of pyrolytic products to biofuels: a novel and sustainable approach toward second-generation biofuels. J. Ind. Microbiol. Biotechnol. 42 (2015) 1557–1579. [DOI] [PMID: 26433384]
5.  Bacik, J.P., Klesmith, J.R., Whitehead, T.A., Jarboe, L.R., Unkefer, C.J., Mark, B.L. and Michalczyk, R. Producing glucose 6-phosphate from cellulosic biomass: structural insights into levoglucosan bioconversion. J. Biol. Chem. 290 (2015) 26638–26648. [DOI] [PMID: 26354439]
[EC 2.7.1.232 created 2021]
 
 
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 3.2.1.220     
Accepted name: ipecoside β-D-glucosidase
Reaction: (1) ipecoside + H2O = ipecoside aglycone + D-glucopyranose
(2) N-deacetylipecoside + H2O = N-deacetylipecoside aglycone + D-glucopyranose
(3) 6-O-methyl-N-deacetylipecoside + H2O = 6-O-methyl-N-deacetylipecoside aglycone + D-glucopyranose
Glossary: ipecoside = methyl (2S,3R,4S)-4-{[(1R)-2-acetyl-6,7-dihydroxy-1,2,3,4-tetrahydro-1-isoquinolinyl]methyl}-2-(β-D-glucopyranosyloxy)-3-vinyl-3,4-dihydro-2H-pyran-5-carboxylate
Other name(s): 6-O-methyl-deacetylisoipecoside β-glucosidase; IpeGlu1
Systematic name: ipecoside glucohydrolase
Comments: The enzyme, isolated from the roots of the plant Carapichea ipecacuanha, preferentially hydrolyses glucosidic ipecoside alkaloids except for their lactams, but shows poor or no activity toward other substrates. IpeGlu1 activity is extremely poor toward 7-O-methyl and 6,7-O,O-dimethyl derivatives. However, 6-O-methyl derivatives are hydrolysed as efficiently as non-methylated substrates. IpeGlu1 accepts both 1α(S)-N-deacetylisoipecoside and 1β(R)-N-deacetylipecoside epimers as substrate, with preference for the 1β(R)-epimer. 6-O-methyl-N-deacetylisoipecoside is an intermediate in the biosynthesis of the medicinal alkaloid emetine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Nomura, T., Quesada, A.L. and Kutchan, T.M. The new β-D-glucosidase in terpenoid-isoquinoline alkaloid biosynthesis in Psychotria ipecacuanha. J. Biol. Chem. 283 (2008) 34650–34659. [DOI] [PMID: 18927081]
[EC 3.2.1.220 created 2023]
 
 
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 3.4.23.2     
Accepted name: pepsin B
Reaction: Degradation of gelatin; little activity on hemoglobin. Specificity on B chain of insulin more restricted than that of pepsin A; does not cleave at Phe1-Val, Gln4-His or Gly23-Phe
Other name(s): parapepsin I; pig gelatinase
Comments: Formed from pig pepsinogen B. In peptidase family A1 (pepsin A family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 9025-48-3
References:
1.  Ryle, A.P. The porcine pepsins and pepsinogens. Methods Enzymol. 19 (1970) 316–336.
[EC 3.4.23.2 created 1961 as EC 3.4.4.2, transferred 1972 to EC 3.4.23.2, modified 1986]
 
 
EC 3.4.23.3     
Accepted name: gastricsin
Reaction: More restricted specificity than pepsin A, but shows preferential cleavage at Tyr┼ bonds. High activity on hemoglobin
Other name(s): pepsin C; pig parapepsin II; parapepsin II
Comments: Formed from progastricsin, apparently in the gastric juice of most vertebrates. In addition to the fundus, progastricsin is also secreted in antrum and proximal duodenum. Seminal plasma contains a zymogen that is immunologically identical with progastricsin [6]. In peptidase family A1 (pepsin A family).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9012-71-9
References:
1.  Ryle, A.P. The porcine pepsins and pepsinogens. Methods Enzymol. 19 (1970) 316–336.
2.  Tang, J. Gastricsin and pepsin. Methods Enzymol. 19 (1970) 406–421.
3.  Foltmann, B. Gastric proteinases - structure, function, evolution and mechanism of action. Essays Biochem. 17 (1981) 52–84. [PMID: 6795036]
4.  Foltmann, B. and Jensen, A.L. Human progastricsin - analysis of intermediates during activation into gastricsin and determination of the amino-acid sequence of the propart. Eur. J. Biochem. 128 (1982) 63–70. [DOI] [PMID: 6816595]
5.  Martin, P., Trieu-Cuot, P., Collin, J.-C. and Ribadeau Dumas, B. Purification and characterization of bovine gastricsin. Eur. J. Biochem. 122 (1982) 31–39. [DOI] [PMID: 6800788]
6.  Reid, W.A., Vongsorasak, L., Svasti, J., Valler, M.J. and Kay, J. Identification of the acid proteinase in human seminal fluid as a gastricsin originating in the prostate. Cell Tissue Res. 236 (1984) 597–600. [PMID: 6432332]
7.  Hayano, T., Sogawa, K., Ichihara, Y., Fujii-Kuriyama, Y. and Takahasi, K. Primary structure of human pepsinogen C gene. J. Biol. Chem. 263 (1988) 1382–1385. [PMID: 3335549]
[EC 3.4.23.3 created 1965 as EC 3.4.4.22, transferred 1972 to EC 3.4.23.3, modified 1986]
 
 


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