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Dsb proteins (DsbA, DsbB, DsbC, and DsbD) catalyze formation and isomerization of protein disulfide bonds in the periplasm of Escherichia coli. DsbC is periplasmic enzyme known as a disulfide isomerase and can convert aberrant disulfide bonds to correct ones.

Biliverdin reductase A (BLVRA) is a member of the gfo/idh/mocA family. BLVRA is an enzyme that converts biliverdin to bilirubin, converting a double-bond between the second and third pyrrole ring into a single-bond. BLVRA reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the simultaneous oxidation of a NADH or NADPH cofactor (Bilirubin + NAD(P)+ = biliverdin + NAD(P)H ).
BLVRA is a regulator for induction of activating transcription factor-2 and heme oxygenase-1. Furthermore, BLVRA enhances the role of HO-1 in cytoprotection and provides cytoprotection independent of heme degradation. In addition, Bilirubin while acting as a cytoprotective antioxidant is itself oxidized to biliverdin and subsequently recycled by biliverdin reductase back to bilirubin.

L-threonine to glycine degradation consists of a two-step biochemical pathway which involvs the enzymes L-threonine dehydrogenase and 2-amino-3-ketobutyrate coenzyme A ligase. L-Threonine is initially converted into 2-amino-3-ketobutyrate by L-threonine dehydrogenase. Glycine C-Acetyltransferase (GCAT) is the 2nd enzyme in this pathway, which subsequently catalyzes the reaction between 2-amino-3-ketobutyrate and coenzyme A to form glycine and acetyl-CoA. The GCAT enzyme is regard as a class II pyridoxal-phosphate-dependent aminotransferase. GCAT is strongly expressed in the heart, brain, liver and pancreas. GCAT is also found in lung.

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.

Uroporphyrinogen III synthase (UROS) is an enzyme involved in the 4th step of porphyrin metabolism and in the conversion of hydroxymethyl bilane into uroporphyrinogen III. Defects in the UROS protein can cause molecular lesions which lead to the autosomal recessive Gunther disease, otherwise known as congenital erythropoietic porphyria (CEP).

Methionine aminopeptidases and designated peptidase M proteins belong to the M24 family of proteins. MAP protein removes the amino-terminal methionine residue from nascent polypeptides. The active site of MAP contains 2 adjacent divalent metal ions connected by a water molecule or hydroxide ion.

Chitodextrinase is a unique membrane-bound endoenzyme. The chitodextrinase enzyme cleaves soluble oligomers, but not chitin, to the di- and trisaccharides. Chitodextrinase is unable to solubilize chitin, but it can catalyze the hydrolysis of high to low molecular weight soluble chitin oligosaccharides.

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.

UBE2V2 comprises a distinct subfamily within the E2 protein family. They have sequence similarity to other ubiquitin-conjugating enzymes however require the conserved cysteine residue that is vital for the catalytic activity of E2s. UBE2V2 shares homology with ubiquitin-conjugating enzyme E2 variant 1 and yeast MMS2 gene product. UBE2V2 participates in the differentiation of monocytes and enterocytes.

Cytosolic and membrane-bound types of GST are encoded by 2 different supergene families. There are 8 classes of the soluble cytoplasmic mammalian GST: alpha, kappa, mu, omega, pi, sigma, theta and zeta. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are arranged in a gene cluster on chromosome 1p13.3 and aare highly polymorphic. These genetic differences can change an individual's resistance to carcinogens and toxins as well as affect the toxicity and efficacy of certain drugs. Null mutations of this class mu gene have been linked with the rise in a number of cancers.

TREX2 holds a 3-prime-to-5-prime exonuclease activity and eliminates mismatched, modified, fragmented, and normal nucleotides to produce the appropriate 3-prime termini for following steps in the DNA metabolic pathways. TREX2 has a role in DNA replication, repair, and recombination.

MMP9 is part of the matrix metalloproteinase family. MMP enzymes take part in the dismantle of extracellular matrix in different physiological pathways, for instance wound healing, bone development, reproduction etc. the enzyme is also involved in pathological pathways: metastasis, arthritis and intracerebral hemorrhage.

NT5M is a member of the 5'(3')-deoxyribonucleotidase family. NT5M localizes to the mitochondrial matrix. The NT5M enzyme dephosphorylates the 5'- and 2'(3')-phosphates of uracil and thymine deoxyribonucleotides. The NT5M gene is located on chromosome 17 p11.2 in the critical region deleted in the Smith-Magenis syndrome (SMS), a genetic disease of unidentified etiology.

Seryl-tRNA synthetase, cytoplasmic (SARS) is a member of the class-II aminoacyl-tRNA synthetase family. Aminoacyl-tRNA synthetases’ role is to catalyze the aminoacylation of tRNAs by their corresponding amino acids, as a result linking amino acids with tRNA-contained nucleotide triplets. The SARS enzyme catalyzes the attachment of serine to tRNA (Ser). SARS enzyme is probably able to aminoacylate tRNA (Sec) with serine, to form the misacylated tRNA L-seryl-tRNA (Sec), which will be then converted into selenocysteinyl-tRNA (Sec).

Diphosphomevalonate decarboxylase (MVD) catalyzes the conversion of mevalonate pyrophosphate into isopentenyl pyrophosphate in one of the early steps in cholesterol biosynthesis. MVD decarboxylates and dehydrates its substrate while hydrolyzing ATP. MVD is expressed in the heart, skeletal muscle, lung, liver, brain, pancreas, kidney and placenta.

ST6GAL1 also known as ST6 Beta-Galactosamide Alpha-2,6-Sialyltranferase 1, is part of the glycosyltransferase family 29. ST6GAL1 is a type II membrane protein which catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. Furthermore, ST6GAL1 is normally found in the Golgi however it can be proteolytically processed to a soluble form, ST6GAL1 is also involved in the generation of the cell-surface carbohydrate determinants as well differentiation antigens HB-6, CD75, and CD76.

Alanine aminotransferase 2 (GPT2), catalyzes the reversible transamination among alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT2 expressed mainly in muscle, fat and kidney and participates in the intermediary metabolism of glucose and amino acids. Multiple transcript variants encoding various isoforms have been found for GPT2.

SORD, also referred to as sorbitol dehydrogenase, belongs to the zinc-containing alcohol dehydrogenase family. It is widely produced. The lens of the eyeand the kidney are the protein highest production areas. Zinc-dependent interconversion of polyols, like sorbitol and xylitol, are enzymatically catalysed to their respective ketoses by SORD.

Glycogen phosphorylase (PYGL) converts from inactive phosphorylase B to active phosphorylase A by phosphorylation of serine residue 15. Activity of the PYGL enzyme is further regulated by numerous allosteric effectors and hormonal controls. The liver isozyme supplies the glycemic demands of the body in general whereas the brain and muscle isozymes supply just those tissues.

MTHFS is a cytosolic protein which takes part in the formate metabolic process. MTHFS along with a magnesium cofactor catalyzes the ATP-dependent reaction which reduces 5-formyltetrahydrofolate (5-MTHF) to 5,10-methenyltetrahydrofolate(MTHF). MTHF is the substrate used by MTHFR (methylenetetrahydrofolate reductase) to generate 5-MTHF. In addition, MTHF is a coenzyme used in thymidine biosynthesis by thymidylate synthase (FAD).

DIM1 dimethyladenosine transferase 1 homolog (DIMT1) is a member of the methyltransferase superfamily. The DIMT1 enzyme specifically dimethylates 2 adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA in the 40S particle. DIMT1 is restricted to the nucleolus.

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.

HMOX2 cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently transferred to bilirubin by biliverdin reductase. Under physiological conditions, the activity of HMOX2 is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. HMOX2 participates in the production of carbon monoxide in the brain where it operates as a neurotransmitter. HMOX2 is an essential enzyme in heme catabolism and is involved in cellular response to oxidative stress.

Lysine Methyltransferase 5A (KMT5A) is an enzyme which catalyzes both histones and non-histone proteins. KMT5A contributes to the maintenance of proper higher-order structure of DNA during mitosis. KMT5A takes part in cell-cycle-dependent transcriptional silencing and mitotic regulation in metazoans. KMT5A plays a role as a barrier to prevent cellular senescence through chromatinmediated regulation of senescence-associated metabolic remodeling. KMT5A mediates monomethylation of p53/TP53 at 'Lys-382', which leads to repress p53/TP53-target genes. The loss of KMT5A simultaneously stimulate nucleolar function and retinoblastoma protein-mediated mitochondrial metabolism.