Catalyzes C14-demethylation of lanosterol which is critical for ergosterol biosynthesis. It transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol. ERG11 Protein, S. cerevisiae, Recombinant (GST) is expressed in E. coli expression system with N-GST tag. The predicted molecular weight is 29.1 kDa and the accession number is P10614.

Catalyzes the biosynthesis of agmatine from arginine.

Essential enzyme in the ergosterol biosynthetic pathway. Part of a 3 enzyme system that catalyzes the sequential removal of the 2 methyl groups at the sterol C-4 position, converting 4,4-dimethylzymosterol to zymosterol. Catalyzes the second step, an oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group. ERG26 Protein, S. cerevisiae, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 46.1 kDa and the accession number is P53199.

Uroporphyrinogen decarboxylase (UROD), is an enzyme of the heme biosynthetic pathway which belongs to the uroporphyrinogen decarboxylase family. This enzyme is responsible for catalyzing the conversion of uroporphyrinogen to coproporphyrinogen through the removal of four carboxymethyl side chains. UROD is a homodimeric enzyme that catalyzes the fifth step in heme biosynthesis: the elimination of carboxyl groups from the four acetate side chains of uroporphyrinogen III to yield coproporphyrinogen III. Defects in UROD are the cause of familial porphyria cutanea tarda (FPCT) and hepatoerythropoietic porphyria (HEP).

Argininosuccinate Synthase (ASS1) is an urea cycle enzyme with a tetrameric structure composed of identical subunits. ASS1 is involved in the synthesis of arginine and catalyzes that condensation of citrulline and aspartate to argininosuccinate using ATP. ASS1 is important to the urea cycle as it catalyzes the important second last step in the arginine biosynthetic pathway. ASS1 mainly expressed in periportal hepatocytes, but also in most other body tissues. A deficiency of ASS1 causes citrullinemia (CTLN1), an autosomal recessive disease which is characterized by severe vomiting spells and mental retardation.

Lysyl oxidase homolog 2, also known as Lysyl oxidase-like protein 2, Lysyl oxidase-related protein 2, Lysyl oxidase-related protein WS9-14 and LOXL2, is a secreted protein that belongs to the lysyl oxidase family. LOXL2 contains four SRCR domains. The lysyl oxidase family is made up of five members: lysyl oxidase (LOX) and lysyl oxidase-like 1-4 ( LOXL1, LOXL2, LOXL3, LOXL4 ). All members share conserved C-terminal catalytic domains that provide for lysyl oxidase or lysyl oxidase-like enzyme activity; and more divergent propeptide regions. LOX family enzyme activities catalyze the final enzymatic conversion required for the formation of normal biosynthetic collagen and elastin cross-links. LOXL2 is expressed by pre-hypertrophic and hypertrophic chondrocytes in vivo, and that LOXL2 expression is regulated in vitro as a function of chondrocyte differentiation. LOXL2 promotes chondrocyte differentiation by mechanisms that are likely to include roles as both a regulator and an effector of chondrocyte differentiation. LOXL2 expression could also be explored as a molecular target in the prevention of breast cancer progression.

Mevalonate kinase belongs to the GHMP kinase family, Mevalonate kinase subfamily. It can be found in a wide variety of organisms from bacteria to mammals. Mevalonate kinase may be a regulatory site in the cholesterol biosynthetic pathway. Defects in mevalonate kinase can cause mevalonic aciduria (MEVA). It is an accumulation of mevalonic acid which causes a variety of symptoms such as psychomotor retardation, dysmorphic features, cataracts, hepatosplenomegaly, lymphadenopathy, anemia, hypotonia, myopathy, and ataxia. Defects in mevalonate kinase can also cause hyperimmunoglobulinemia D and periodic fever syndrome (HIDS). HIDS is an autosomal recessive disease characterized by recurrent episodes of unexplained high fever associated with skin rash, diarrhea, adenopathy (swollen, tender lymph nodes), arthralgias, and/or arthritis.

The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is mainly involved in the biosynthetic transport of proteins from the Golgi to the plasma membrane. Regulates, for instance, SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane. In parallel, it regulates the transport of TLR4, a toll-like receptor to the plasma membrane and therefore may be important for innate immune response. Plays also a specific role in asymmetric protein transport to the plasma membrane. In neurons, it is involved in axonogenesis through regulation of vesicular membrane trafficking toward the axonal plasma membrane. In epithelial cells, it regulates transport from the Golgi to the basolateral membrane. May play a role in the basolateral recycling pathway and in phagosome maturation. May play a role in endoplasmic reticulum dynamics and morphology controlling tubulation along microtubules and tubules fusion. Together with LRRK2, RAB8A, and RILPL1, it regulates ciliogenesis. When phosphorylated by LRRK2 on Thr-73, it binds RILPL1 and inhibits ciliogenesis.

Porphobilinogen Deaminase (HMBS) is a member of the HMBS family. PBGD is the third enzyme of the heme biosynthetic pathway and catalyzes the head to tail condensation of four porphobilinogen molecules into the linear hydroxymethylbilane. HMBS is involved in the production of heme, which is important for all of the body's organs, although it is most abundant in the blood, bone marrow, and liver. In addition, Heme is an essential component of iron-containing proteins called hemoproteins, including hemoglobin. Defects in PBGD are the cause of acute intermittent porphyria.

BBOX1, also known as gamma-BBH, belongs to thegamma-BBH/TMLD family. It is highly expressed in kidney and moderately expressed in liver. BBOX1 catalyzes the formation of L-carnitine from gamma-butyrobetaine, the last step in the L-carnitine biosynthetic pathway. Carnitine is essential for the transport of activated fatty acids across the mitochondrial membrane during mitochondrial beta-oxidation. BBOX1 is an inhibition target for mildronate which can be used to treatanginaandmyocardial infarction. Mildronate may also be beneficial for the treatment ofneurological disorder,diabetes, andseizures andalcohol intoxication.

Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.

A cytochrome P450 monooxygenase that plays a major role in adrenal steroidogenesis. Catalyzes the hydroxylation at C-21 of progesterone and 17alpha-hydroxyprogesterone to respectively form 11-deoxycorticosterone and 11-deoxycortisol, intermediate metabolites in the biosynthetic pathway of mineralocorticoids and glucocorticoids. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase).

Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. PFAS Protein, Human, Recombinant (His & Myc & SUMO) is expressed in E. coli expression system with N-10xHis-SUMO and C-Myc tag. The predicted molecular weight is 45.4 kDa and the accession number is O15067.

A cytochrome P450 monooxygenase that plays a major role in adrenal steroidogenesis. Catalyzes the hydroxylation at C-21 of progesterone and 17alpha-hydroxyprogesterone to respectively form 11-deoxycorticosterone and 11-deoxycortisol, intermediate metabolites in the biosynthetic pathway of mineralocorticoids and glucocorticoids. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase).

7-dehydrocholesterol reductase of the cholesterol biosynthetic pathway reducing the C7-C8 double bond of cholesta-5,7-dien-3beta-ol (7-dehydrocholesterol/7-DHC) and cholesta-5,7,24-trien-3beta-ol, two intermediates in that pathway. DHCR7 Protein, Bovine, Recombinant (His) is expressed in E. coli expression system with N-10xHis tag. The predicted molecular weight is 55.8 kDa and the accession number is Q5E9J5.

The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinons involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis. NQO1 Protein, Mouse, Recombinant (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 32.8 kDa and the accession number is Q64669.

The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis.

NAD Kinase (NADK) is an enzyme that belongs to the NAD Kinase family. It is a widely expressed enzyme, but it is not detected in skeletal muscle. NADK converts Nicotinamide Adenine Dinucleotide (NAD+) into NADP+, through phosphorylating the NAD+ coenzyme. NADP+ is an essential coenzyme in metabolism and provides reducing power to biosynthetic processes such as fatty acid biosynthesis. The structure of the NADK from the archaean Archaeoglobus fulgidus has been determined.

Sialic Acid Synthase (NANS) is an enzyme that contains one AFP-like domain. NANS is ubiquitous and plays a role in the biosynthetic pathways of sialic acids. NANS produces N-acetylneuraminic acid (Neu5Ac) and 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN). It also can use N-acetylmannosamine 6-phosphate and mannose 6-phosphate as substrates to generate phosphorylated forms of Neu5Ac and KDN, respectively.

NAD(P)+transhydrogenase (NNT) is located in the inner mitochondrial membrane and catalyzes a reversible hydride transfer between NAD(H) and NADP(H) that is coupled to proton translocation between the intermembrane space and mitochondrial matrix. NNT activity has an essential role in maintaining the NADPH supply for antioxidant defense and biosynthetic pathways. Structurally, NNT is composed of three domains; domains I and III are hydrophilic and have binding sites for NAD and NADP, respectively, while domain II is hydrophobic and is a transmembrane pathway through which protons translocate. NNT forms dimers, whose monomers act in an anti-phase way; domain III (NADP(H)- binding) flips, allowing proton translocation across the inner mitochondrial membrane one moment and favoring hydride transfer between NAD(H) and NADP(H) the next. And NNT pathophysiological roles after the discovery of a spontaneous Nnt mutation in C57BL/6J mice. And Nnt silencing reduced the growth of cancer cell lines, suggesting that NNT might be a therapeutic target in some cancers.

PMVK is a peroxisomal enzyme that catalyzes the conversion of mevalonate 5-phosphate into mevalonate 5-diphosphate, the fifth reaction of the cholesterol biosynthetic pathway. Studies in rat show that the message level and the enzyme activity of PMVK is regulated by sterol, and that this regulation is coordinated with 3-hydroxy-3-methylglutaryl coenzyme A reductase, the rate-limiting enzyme of cholesterol biosynthesis.