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SAE1 and SAE2 form heterodimers which take part in the posttranslational modification of proteins (sumoylation). This process regulates protein structure as well as intracellular localization of the target. SAE1/SAE2 may indicate on dermatomyositis (DM) as autoantibodies against those 2 proteins have been found in patients.

Yersinia enterocolitica is a Gram-negative bacillus-shaped bacterium, which is a member of the Enterobacteriaceae family. Y.Enterocolitica is motile at temperatures between 22-29°C, however becomes non-motile at normal human body temperature. Y. Enterocolitica infection causes the yersiniosis disease, which is an animal-borne disease occurring in humans, as well as in a various groups of animals such as cattle, deer, pigs, and birds. Yersinia enterocolitica is a heterogeneous group of strains, which are conventionally classified by bio-typing into six bio-groups on the basis of phenotypic characteristics, and by serotyping into more than 57 “O” serogroups, on the basis of their O (lipopolysaccharide or LPS) surface antigen. Five of the six biogroups (1B and 2–5) are considered as pathogens. Nevertheless, only a few of these serogroups have been linked with disease in either humans or animals. Strains which belong to serogroups O:3 (biogroup 4), O:5,27 (biogroups 2 and 3), O:8 (biogroup 1B), and O:9 (biogroup 2) are most frequently isolated worldwide from human samples. Still, the main Y. enterocolitica serogroup in many European countries is serogroup O:3 followed by O:9, whereas the serogroup O:8 is mostly detected in the United States.

Dopa decarboxylase is a homodimeric, pyridoxal phosphate dependent enzyme.
Dopa decarboxylase is involved in 2 metabolic pathways, synthesizing 2 significant neurotransmitters the take part in numerous clinical disorders, including Parkinson’s disease. Dopa decarboxylase is located in different areas of the brain and is mostly found in basal ganglia. Dopa decarboxylase catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (DOPA) to dopa, L-5-hydroxytryptophan to serotonin and L-tryptophan to tryptamine. Defects in Dopa decarboxylase leads to aromatic L-amino-acid decarboxylase deficiency (AADCD). AADCD deficiency is an inborn error in neurotransmitter metabolism that causes combined serotonin and catecholamine deficiency.

Adenosine deaminase-like protein (ADAL) is a putative nucleoside deaminase. ADAL catalyzes the hydrolytic deamination of adenosine or some similar substrate and has a role in purine metabolism.

Endothelin-2 is a Hypoxia-induced Autocrine Survival Factor for Breast Tumor Cells. The synthesis of EDN2 by human kidney carcinoma cells is decreased by EGF. EDN2 is a chemoattractant for macrophages and THP-1 monocytic cells. Chemotaxis towards EDN2 is via the MAPK pathway: p44 and p42 are phosphorylated when THP-1 cells are stimulated with EDN2. Migration to EDN2 is inhibited by hypoxia and by pertussis toxin. EDN2 leads to activation of macrophages. EDN2 shares a similar peptide sequence with chemokines and may signal via a similar receptor and MAPK-mediated pathway. Furthermore, EDN2 expression by tumors may modulate the behavior of macrophages such that activated cells accumulate in areas of hypoxia.

GOT1 is a pyridoxal phosphate-dependent enzyme which exists in cytoplasmic and mitochondrial forms, GOT1 and GOT2, which participate in amino acid metabolism and the urea and tricarboxylic acid cycles. Both enzymes are homodimeric and show close homology.

Membrane-bound & Cytosolic forms of GST are encoded by 2 separate supergene families. These enzymes function in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. There are 8 different classes of soluble cytoplasmic mammalian GST: alpha, kappa, mu, omega, pi, sigma, theta and zeta. The GSTA1 is found in a cluster mapped to chromosome 6, and is highly expressed in the liver. GSTA1 protects the cells from reactive oxygen species.

Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene is a cytoplasmic enzyme which belongs to the class II family of aminoacyl-tRNA synthetases. The enzyme is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of histidine into proteins. The gene is located in a head-to-head orientation with HARSL on chromosome five, where the homologous genes share a bidirectional promoter. The gene product is a frequent target of autoantibodies in the human autoimmune disease polymyositis/dermatomyositis.

PGAM1 is part of the phosphoglycerate mutase family. PGAM1 is an essential component of glucose and 2,3-BPGA (2,3-bisphosphoglycerate) metabolism and catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway. PGAM1 is a dimeric enzyme containing, in different tissues, different proportions of a slow-migrating muscle (MM) isozyme, a fast-migrating brain (BB) isozyme, and a hybrid form (MB). PGAM1 mutations lead to muscle phosphoglycerate mutase deficiency, a.k.a. glycogen storage disease X.

Lysozymeis an antimicrobial enzyme produced by animals that are part of the innate immune system. Lysozyme is a glycoside hydrolase that catalyzes the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycan, which is the major component of gram-positive bacterial cell wall.Lysozymes have primarily a bacteriolytic function - those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.

GALE is an enzyme that participates as the third enzyme in the Leloir pathway of galactose metabolism. GALE is a homodimeric epimerase localized in bacterial, plant, and mammalian cells. GALE inhances the reverse chemical reaction, the conversion of UDP-glucose to UDP-galactose. UDP-galactose builds galactose-containing proteins and fats, which have a crucial part in chemical signaling, building cellular structures, transporting molecules, and producing energy.

NAA10 is a member of the acetyltransferase family. NAA10 interacts with NAA15, HIF-1 and with the ribosome. In its binding to HIF-1, NAA10 functions as a protein acetyltransferase by regulating its stability. In various cell lines, NAA10 is downregulated in response to hypoxia. NAA10 is expressed during the course of the development of the brain.

Thioredoxin reductase (TrxR/NTR), an enzyme belonging to the flavoprotein family of pyridine nucleotide-disulfide oxidoreductases. Thioredoxin reductase (TrxR), a component of the thioredoxin system, including thioredoxin (Trx) and NADPH, catalyzes the transfer of electrons from NADPH to Trx, acts as a reductant of disulfide-containing proteins and participates in the defense system against oxidative stresses.

Glycolate oxidase (HAO1) belongs to the superfamily of the alpha hydroxy acid oxidases (HAO) enzymes. HAO1 catalyzes the FMN mediated oxidation of glycolate to glyoxylate and glyoxylate to oxalate with reduction of oxygen to hydrogen peroxide. HAO1 is most abundantly expressed in the liver and pancreas and is most active on twocarbon substrates such as glycolate. Lately, HAO1 has been identified as a key contributor to hyperoxaluria, a disorder in which large deposits of calcium oxalate form kidney stones.

Yersinia enterocolitica is a Gram-negative bacillus-shaped bacterium, which is a member of the Enterobacteriaceae family. Y.Enterocolitica is motile at temperatures between 22-29°C, however becomes non-motile at normal human body temperature. Y. Enterocolitica infection causes the yersiniosis disease, which is an animal-borne disease occurring in humans, as well as in a various groups of animals such as cattle, deer, pigs, and birds. Yersinia enterocolitica is a heterogeneous group of strains, which are conventionally classified by bio-typing into six bio-groups on the basis of phenotypic characteristics, and by serotyping into more than 57 “O” serogroups, on the basis of their O (lipopolysaccharide or LPS) surface antigen. Five of the six biogroups (1B and 2–5) are considered as pathogens. Nevertheless, only a few of these serogroups have been linked with disease in either humans or animals. Strains which belong to serogroups O:3 (biogroup 4), O:5,27 (biogroups 2 and 3), O:8 (biogroup 1B), and O:9 (biogroup 2) are most frequently isolated worldwide from human samples. Still, the main Y. enterocolitica serogroup in many European countries is serogroup O:3 followed by O:9, whereas the serogroup O:8 is mostly detected in the United States.

A main factor of pathogenic Yersinia enterocolitica strains is a plasmid-encoded type 3 secretion system, through which Yersinia outer proteins (Yops) are injected into the host cell. Yop E is a GTPase activation protein which controls pore formation by activating small Rho GTPase, causing inhibition of actin polymerization.

Ribonuclease 7 (RNASE7) is one of the final RNase A superfamily ribonucleases. RNASE7 was isolated from skin-derived stratum corneum. RNASE7 protein demonstrated potent ribonuclease activity and hence may contribute to the well-known ribonuclease activity of human skin. RNASE7 has revealed a broad spectrum antimicrobial activity against many pathogenic microorganisms and extraordinarily potent activity.

Human Ubquitin Conjugating Enzyme 7 (UbcH7) is a class I enzyme which functions in the stress response and the control of transcription factors. The enzyme is ubiquitously expressed with high levels of expression seen in adult muscle. UbcH7 mediates the selective degradation of short-lived and abnormal proteins and is highly homologous to UbcH5. It has been demonstrated to participate in the ubiquitinylation of p53, c-Fos and NF-?B. UbcH7 is one of two E2s (UbcH5 being the other) with which HECT domain proteins interact with UbcH7 being able to efficiently substitute for UbcH5 in E6-AP-dependent ubiquitinylation.

Peptide methionine sulfoxide reductase A (msrA) is an enzyme which catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. MSRA may have a significant function as a repair enzyme for proteins which have been inactivated by oxidation.

FOLH1, also known as glutamate carboxypeptidase 2 (GCPII), is a single pass type 2 membrane protein which belongs to the peptidase M28 family. FOLH1 is highly produced in prostate epithelium. FOLH1 is also found in ovary, live, stomach, small intestine colon, urinary bladder, kidney, testis, and the capillary endothelium of a variety of tumours. Therefore, it plays a role in directed imaging and therapy of recurrent of metastatic disease. FOLH1 is a zinc metalloenzyme that resides in membranes and catalyses the hydrolysis of N-acetylaspartylglutamate to glutamate and N-acetylaspartate.

Lysyl Oxidase also known as LOX is an extracellular copper enzyme which initiates the crosslinking of collagens and elastin. LOX catalyzes oxidative deamination of the epsilon-amino group in certain lysine and hydroxylysine residues of collagens and lysine residues of elastin. Adding up to crosslinking extracellular matrix proteins, LOX plays a part in tumor suppression. Moreover, defects in LOX are the cause of autosomal recessive cutis laxa type I, CL type I. Two transcript variants encoding dissimilar isoforms have been found for LOX.

Human Ubquitin-conjugating enzyme 7 (UbcH7) is a ubiquitin-conjugating enzyme (E2) mediating c-fos degradation, transcription factor NF-B maturation, and human papilloma virus-mediated p53 and Myc protein degradation, in vitro. The ubiquitin-conjugating enzymes (E2s) are essential components of the post-translational protein ubiquitination pathway, mediating the transfer of activated ubiquitin to substrate proteins. The human UBE2L1-UBE2L4 gene could potentially encode different isoforms of the UbcH7. UBE2L3 gene, located at chromosome 22q11.2, is the only identical family member with introns and encodes a polypeptide sequence identical to that of UbcH7.

Thiosulfate sulfurtransferase (glpE) is a mitochondrial matrix enzyme which is encoded by the nucleus. Escherichia coli glpE is a prototype for the single-domain rhodanese superfamily. glpE catalyzes the sulfur-transfer reaction in which a sulfur atom is transferred from thiosulfate to cyanide by a double-displacement mechanism.

DAAO is a peroxisomal enzyme which uses FAD (flavin adenine dinucleotide) as a cofactor and oxidizes D-amino acids to the corresponding amino acids, producing ammonia and hydrogen peroxide. DAAO substrates include an extensive array of D-amino acids, but it is inactive on the naturally occurring L-amino acids. DAAO acts on a variety of D-amino acids especially on those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups; however it doesn’t act on acidic amino acids. DAAO may be involved in acid base balance in the kidney or it could act as a detoxifying agent which removes D-amino acids accumulated during aging. DAAO regulates the neuromodulator D-serine level in the brain. DAAO is highly active towards D-DOPA. Creatinine inhibits the DAAO in uremia. DAAO may also have a role in the pathophysiology of schizophrenia, but not in bipolar disorder.